Антикоагулянтная активность низкомолекулярных гепаринов, полученных с помощью гидролаз
Коммерческие НМГ (Nadroparin calcium (Fraxiparin), Certoparin. Dalteparin sodium (Fragmin), Enoxaparin sodium (Clexane), Nadroparin, Reviparin, Tinzaparin) имеют среднюю молекулярную массу 3,5−6,0 кДа, и используются для профилактики и лечения тромбозов глубоких вен. венозных тромбоэмболии, инфаркта миокарда, тромботического инсульта, порока сердца, тяжелых заболеваниях легких, при лечении… Читать ещё >
Содержание
- Список сокращений
- 1. Обзор литературы
- 1. 1. Современные антикоагулянтные средства
- 1. 2. Антикоагулянтная активность сульфатированных полисахаридов
- 1. 3. Гепарин
- 1. 3. 1. Биосинтез гепарина
- 1. 3. 2. Выделение гепарина
- 1. 3. 3. Строение и антикоагулянтная активность гепарина
- 1. 3. 4. Деполимеризация гепарина
- 1. 3. 5. Нейтрализация антикоагулянтной активности гепарина
- 3. 1. Антикоагулянтная активность фракций низкомолекулярного гепарина (НМГ) фирмы «Selsus lab»
- 3. 2. Антикоагулянтная активность НМГ, полученного экструзионной деполимеризацией нефракционированного гепарина (НФГ)
- 3. 3. Антикоагулянтная активность НМГ, полученных с помощью ферментативных способов гидролиза нефракционированпых гепаринов
- 3. 3. 1. Антикоагулянтная активность НМГ, полученных с помощью гидролиза
3.3.1.1. Антикоагулянтная активность НМГ, полученных с помощью гидролиза иммобилизованным ферментным комплексом Streptomycess kurssanovii НФГ из легких крупного рогатого скота (Московский эндокринный завод).
3.3.1.2. Антикоагулянтная активность НМГ, полученных с помощью гидролиза иммобилизованным ферментным комплексом Streptomycess kurssanovii НФГ из кишечника свиней (Changzhou quianhong bio-pharm со Ltd, Китай).
3.3.1.3. Сравнение ангикоагулянтной активности Са+3 модификацикаций НФГ (ОАО «Белмедпрепарат») из легких крупного рогатого скота и его гидролизованиых с помощью ферментного комплекса Streptomycess kurssanovii фракций.
3.3.1.4. Антикоагулянтная активность гидролизатов разных по времени партий НФГ (Changzhou quianhong bio-pharm со Ltd, Китай) из слизистой оболочки кишечника свиней, полученных ферментативной деполимеризацией.
3.3.1.5. Влияние НМГ-4,7 кДа на генерацию тромбина in vitro.
3.3.2. Антикоагулянтная активность образцов НМГ, полученных с помощью гидролиза НФГ ферментным комплексом препарата Протеаза С.
3.3.2.1. Антикоагулянтная активность НМГ. полученных с помощью гидролиза НФГ (ООО '"Синтез") из легких крупного рогатого скота.
3.3.2.2. Антикоагулянтная активность НМГ, полученных с помощью гидролиза НФГ (АО «Синтез») из легких крупного рогатого скота иммобилизованной Протеазой С в разных соотношениях.
3.3.3. Антикоагулянтная активность образцов НМГ, полученных с помощью деполимеризации НФГ гидролазами.
3.3.3.1. Антикоагулянтная активность образцов НМГ. полученных с помощью деполимеризации НФГ (ОАО «Белмедпрепарат») из легких крупного рогатого скота папаином, целловиридином, химотрипсином.
3.3.3.2. Антикоагулянтная активность НМГ с ММ 3,4- 4,1 и 5,1 кДа, полученных с помощью гидролиза химотрипсином в растворе НФГ (Changzhou quianhong bio-pharm со Ltd, Китай) из слизистой оболочки кишечника свиней.
3.3.3.3. Антикоагулянтная активность НМГ, полученных с помощью гидролиза иммобилизованным химотрипсином НФГ (Changzhou quianhong bio-pharm со Ltd, Китай) из слизистой оболочки кишечника свиней.
3.3.3.4. Антикоагулянтная активность НМГ. полученных гидролизом папаина НФГ (Changzhou quianhong bio-pharm со Ltd, Китай) из слизистой оболочки кишечника свиней.
3.3.3.5. Антикоагулянтная активность НМГ, полученных с помощью гидролиза иммобилизованным папаином НФГ (ОАО «Белмедпрепарат») из легких крупного рогатого скота.
3.3.4. Антикоагулянтная активность НМГ, полученных деполимеризацией НФГ лизоцимом.
3.3.4.1. Антикоагулянтная активность НМГ, полученных деполимеризацией НФГ (ОАО «Белмедпрепарат») и его Са +2 модификации с помощью лизоцима.
3.3.4.2. Сравнение антикоагулянтной активности НМГ, полученных гидролизом лизоцимом и ферментным препаратом Протеаза С НФГ (ОАО «Белмедпрепарат»).
3.3.4.3. Антикоагулянтная активность НМГ, полученных гидролизом НФГ (ОАО «Белмедпрепарат») иммобилизованным лизоцимом и лизоцимом в растворе.
3.4. Влияние НМГ-7,0 кДа (гидролиз лизоцимом) и НМГ-9,0 кДа (гидролиз ферментным комплексом Протеаза С) на агрегацию тромбоцитов человека in vitro.
3.5. Исследование образования комплексов между полианионами НМГ и поликатионами.
3.5.1. Биоспецифичиый электрофорез комплексов НМГ (полученных гидролизом НФГ ферментным комплексом Streptomycess kurssanovii) с поликатионами.
3.5.2. Биоспецифичный электрофорез комплексов НМГ (полученных гидролизом НФГ ферментным комплексом Протеаза С) с сульфатом протамина.
3.5.3. Нейтрализация антикоагулянтной активности образцов НМГ.
3.5.3.1. Нейтрализация антитромбиновой активности НМГ в тесте АЧТВ.
3.5.3.2. Нейтрализация сульфатом протамина ингибирования гепаринами амидолитической активности тромбина.
3.5.3.3. Нейтрализация ингибирования гепаринами амидолитической активности фактора Ха сульфатом протамина.
3.6. Фармакодинамические и фармакокинетические параметры низкомолекулярных гепаринов, полученных с помощью ферментативного гидролиза НФГ.
3.6.1. Фармакодинамические и фармак0кине1ические параметры НМГ с ММ 4,7 кДа (НМГ- 4,7), полученного с помощью гидролиза НФГ ферментным комплексом Slreptomycess knrssanovii.
3.6.1.1. Влияние НМГ-4,7 на время свертывания плазмы кроликов при внутривенном введении.
3.6.1.2. Влияние НМГ-4,7 на время свертывания плазмы кроликов при подкожном введении.
3.6.2. Фармакодинамические и фармакокинетические параметры низкомолекулярного гепарина с ММ 5,4 кДа, полученного с помощью гидролиза НФГ ферментным комплексом Протеаза С.
3.6.2.1. Влияние НМГ-5,4 на время свертывания плазмы кроликов при внутривенном введении.
3.6.2.2. Влияние НМГ-5,4 на время свертывания плазмы кроликов при подкожном введении.
3.6.3. Влияние НМГ с ММ 7 кДа, полученного гидролизом лизоцимом НФГ на время свертывания плазмы кроликов при подкожном введении.
3.7. Антитромботическая активность низкомолекулярных гепаринов, полученных с помощью гидролиза НФГ ферментным комплексом Streptomycess kurssanovii (НМГ-4,7) и Протеаза С (НМГ-5,4).
3.8. Геморрагическая активность низкомолекулярных гепаринов, полученных с помощью гидролиза НФГ ферментным комплексом Streptomycess kurssanovii (НМГ-4,7) и Протеаза С (НМГ-5.4).
3.9. Влияние НМГ-4,7 кДа и НМГ-5.4 кДа на активность протеина С плазмы кроликов в результате подкожного введения.
3.10. Влияние НМГ-4,7 кДа и НМГ-5,4 кДа на активность плазминогена плазмы кроликов в результате подкожного введения.
4. Обсуждение.
Выводы.
Список литературы
- Баранов Г. А., Беляев А. А. Оникиеико С.Б. и др. Взаимодействие луча С02 с падающей каплей жидкости при модификации растворенных в ней биообъектов// Письма в ЖТФ.- 2003, — Т.29, — В. 13, — С.57−63
- Баркаган З. С. Момот А. П. «Диагностика и контролируемая терапия нарушений гемостаза» Москва.: Ньюдиамед 2001 — 74с.
- Бернхард С., «Структура и функция ферментов, пер. с англ.» Москва.: Мир 1971.
- Введение в прикладную этимологию. Иммобилизованные ферменты, под ред. И. В. Березина, К. Мартинека Москва.: Мир 1982.
- Государственная Фармакопея СССР XI издание, том 1. статья 42−1256−79
- Дрозд Н.Н., Макаров В. А., Башков Г. В. и др. Влияние совместного введения гепарина и сернокислого эфира хитозана на функцию гемостаза // Экспериментальная и клиническая фармакология. 1996. — № 59, — В.1.- С. 30−33.
- Дрозд Н.Н., Толстенков А. С., Макаров В. А., Банникова Г. Е., Варламов В. П., Скрябин К. Г. Способ обнаружения комплексов между гепаринами и поликатионами. Патент РФ № 2 006 141 290, опубл. 27.05.2008 Бюл. № 15
- Ермак И. М. Соловьева Т.Ф. «Сборник инвестиционных предложений I Международного инвестиционного конгресса „Новейшие технологии в системе интегральных процессов территорий стран АТР“» Владивосток, — 2000, — С. 276.
- Заиков Г. Е. Деструкция и стабилизация полимеров. Москва.: МИТХТ им. М. В. Ломоносова, 1993.-248с.
- Ильина А.В., Варламов В. П. Ферментативная деполимеризация N-сукцинилхитозана //Биоорг. Хим. -2007, — № 33, — В.1.- С. 156−159.
- И. Ильина А. В., Татарипова Н. Ю., Тихонов В. Е., Варламов В.П.// Внеклеточные протеаза и хитиназа, продуцируемые культурой Streptomyces kurssanovii // Прикладная биохимия и микробиология.- 2000, — Т. 36. № 2, — С. 184−188.
- Иммобилизованные ферменты. Современное состояние и перспективы, под ред. И. О. Березина.- Москва.: Изд-во МГУ 1976,-т. 1−2.
- Козлов Л. В., «Биоорганическая химия» Москва: Наука 1980, — т. 6, — № 8.- с. 1243−54.
- Козлов Л. В.- Введение в прикладную энзимологию: Учебное пособие / Под. Ред. ИВ Березина и К Мартинека М.: Изд-во Моск. Универ, 1982 — С 384
- Максименко А.В., Тищенко Е. Г., Голубых В. Л. Аптитромботическое действие производных каталазы и хондроитинсульфата при артериальном поражении у крыс// Вопр Мед Хим.- 1999, — Т 45, — № 6, — С. 20−25.
- Мосолов В. В. «Протеолитические ферменты», Москва: Наука 1971.
- Назаров И.В., Шевченко Н. М. Ковалев Б.М., Хотимченко Ю. С. Действие на систему комплемента полисахаридов из красных водорослей. // Биология моря, — 1998.- т. 24, — № 1.-С.50−53.
- Никитин В.М., Оболенская А. В., Щеголев В.П." Химия древесины и целлюлозы", М.: Лесная промышленность, 1978.- С. 75−78.
- Нортроп Д., Кунитц М., Херриотт Р. «Кристаллические ферменты, пер. с англ» М.: Наука 1950.
- Прикладная статистика. Исследование зависимостей: Справ. Изд./ С. А. Айвазян, И. С. Енюков, Л.Д. Мешалкин- Под ред. С. А. Айвазяна. М.: Финансы и статистика, 1985.- С 61.
- Струкова С.М. Нарушения в системе протеина С у больных с антифосфолипидным синдромом // Тромбозы, кровоточивость и болезни сосудов.- 2002, — № 2, — С. 21−26.
- Тривен ML «Иммобилизованные ферменты. Вводный курс и применение в биотехнологии» М. Мир 1983.
- Тюкавкина Н.А., Ю.И. Бауков «Биоорганическая химия» издание второе, переработанное и дополненное. М.: Медицина, 1991
- Уайт А. Хендлер Ф. Смит Э. Хилл Р. Леман И., Основы биохимии. М.: Мир.- 1981.
- Усов, А И., Смирнова Г. II, Билап М. И., Шашков А. С., Структурные особенности фукоиданов // Биоорг. Химия 1998, — Т. 24, — № 6.- С.437−445.
- Филлипс Д., «Трехмерная структура молекулы фермента, в сборнике: Молекулы и клетки, пер. с англ» М.: Мир 1968.- В 3.
- Химия белка, сборник статей / Под. ред. М. М. Ботвинник.-М.: Мир, 1969.
- Чазов Е.И., Лаким К. М. Ан гикоагуляпты и фибринолшические средства// Москва: Медицина, 1977, — С. 172−185
- Чевари С.И., Чаба С. А. Спектрофотометрический метод определения гемоглобина в крови // Лаб. дело.- 1985, — № 8, — С.457−460.
- Abatangelo G., Barbucci R., Brun P., Lamponi S. Biocompatibility and enzymatic degradation studies on sulphated hyaluronic acid derivatives // Biomaterials. 1997.- V.18.- № 21.-P. 1411−1416.
- Adler B.K. Unfractionated heparin and other antithrombin mediated anticoagulants // Clin Lab Sci. 2004, — V. 17.- № 2, — P. 113−120.
- Ahsan A. Jeske W., Hoppensteadt D., et al. Molecular profiling and weight determination of heparins and depolymerized heparins // J. Pharm. Sci. 1995.- № 84.- P.724−727.
- Alban S., Gastpar R. Plasma levels of total and free tissue factor pathway inhibitor (TFPI) as individual pharmacological parameters of various heparins // Thromb Haemost.- 2001, — № 85.- P. 824−829.
- Albuquerque I.R., Queiroz K.C., Alves L.G., et al. Heterofucans from Dictyota menstrualis have anticoagulant activity // Braz. J. Med. Biol. Res.- 2004, — V.37.- № 2, — P. 167−171.
- Alderman E.L., Levy J.H., Rich J.B., et al. Analyses of coronary graft patency after aprotinin use: results from the International Multicenter Aprotinin Graft Patency Experience (IMAGE) trial //J Thorac Cardiovasc Surg.- 1998.- №.116.- P.716−746.
- Amiral J., Bridey F., Dreyfus M.,'et al. Platelet factor 4 complexed to heparin is the target for antibodies generated in heparin induced thrombocytopenia // Thromb. Haemost.- 1992, — №.68.-P.95−101.
- Andrade-Gordon P., Strickland S. Interaction of heparin with plasminogen activators and plasminogen: effects on the activation of plasminogen // Biochemistry.- 1986.- №.25, — P. 40 334 073.
- Anthony C. Leslie В., Hugh O’B., et al. Covalent Antithrombin-Heparin Complexes with High Anticoagulant Activity // J Biol Chem.- 1997, — V.272.- № 35, — P.22 111−22 117.
- Bal dit Sollier C., Kang C., Berge N. et al. Activity of a synthetic hexadecasaccharide (SanOrgl23781 A) in a pig model of arterial thrombosis // M. Journal of Thrombosis and Haemostasis.- 2004.- V2.- № 6.- P.925−930.
- Bara L. Samama M.M. Pharmacokinetics of low molecular weight heparins // Acta Chir Scand.- 1988.- №.543, — P.65−72.
- Barbanti M, Calanni F. Marchi E. et al. A low molecular weight dermatan sulphate, reduces the weight of preformed thrombi in rats made afibrinogenemic by ancrode.// Thrombosis haemost.- 1995, — V73.-№ 2.- P. 287−377.
- Barbucci R., Lamponi S., Magnani A, Renier D. The influence of molecular weight on the biological activity of heparin like sulphated hyaluronic acids// Biomaterials.- 1998.- №.19.- P.801−807.
- Barrow R.T., Parker E T, Krishnaswamy S. and Lollar P. Inhibition by heparin of the human blood coagulation intrinsic pathway factor X activator // J. Biol. Chem.- 1994.- V.269.-№ 43.- P.26 796−26 800.
- Barrowcliffe T.W., Mulloy В., Johnson E.A., Thomas D.P. The anticoagulant activity of heparin: measurement and relationship to chemical structure // Circulation.- 2001, — V.7.- № 2.-P.2994−3018.
- Ba§ ar N, Uzun L, Giiner A, Denizji A. Lysozyme purification with dye-affinity beads under magnetic field // International Journal of Biological Macromolecules 2007, — V.41.- № 3.- P.234−242.
- Bates S.M., Weitz J.I. Coagulation Assays // Circulation. 2005. -V 112, — N 4. P 53−60.
- Bedford RF and ТЕ O’Brien Comparison of bovine lung and porcine intestinal heparin for arterial thrombosis in man American // Journal of Hospital Pharmacy.- 1977.- V.34.- №. 9.-P.936−939 .
- Bendayan P, Boccalon H, Dupouy D. Boneu B. Dermatan sulfste is a more potent inhibitor of clot-bound thrombin than unfractionated and low molecular weight heparins // Thromb Haemost.- 1994, — V.71.-№ 5.- P.576−656.
- Bentolila A. Vlodavsky I., Ishai-Michaeli R., et al. Poly (N-acryl amino acids): a new class of biologically active polyanions // Med. Chem.- 2000, — V.43.- № 13.- P.2591−2600.
- Bergqvist D. Nilsson В., Hedner U., et al. The effects of hepaiin fragments of different molecular weight in experimental thrombpsis and hacmostasis // Thromb. Res.- 1985.- V38.-№ 6.-P.589−601.
- Bernard G.R. Vincent J.L., Lalerre P.F., et al. Efficacy and safety of lecombinant human activated protein С for severe sepsis //N Engl J Med.- 2001.- V.344.- № 10 P.699−709.
- Bcrteau O, Mulloy В Sulfated fucans, fresh perspectives: structures, functions, and biological properties of sulfated fucans and an overview of enzymes active toward this class of polysaccharide //Glycobiology.- 2003,-V.13.-№ 6.-P.29−40.
- Bianchini P., Liverani L., Mascellani G., Parma B. Heterogeneity of unfractionated heparins studied in connection with species, souice, and production processes // Semin Thromb Hemost.- 1997, — V.23.- № 1.- P.3−10.
- Bianchini P., Liverani L., Spelta F., et al. Variability of Heparins and Heterogeneity of Low Molecular Weight Heparins // Seminars in Thrombosis and Haemostasis.- 2007.- V. 33, — № 5.-P.- 496−502.
- Bijsterveld, Nick R., Vink et al. Recombinant factor Vila reverses the anticoagulant effect of the long-acting pentasaccharide idraparinux in healthy volunteers // British Journal of Haematology.- March 2004, — V.124.- № 5, — P.653−658.
- Bilan M.I., Grachev A.A., Ustuzhanina N.H., et al. Structure of a fucoidan from the brown seaweed Fucus evanescens C.Ag.//Carbohydr. Res.- 2002, — V.337.- № 8, — P. 719−730.
- Bisio A. Guglieri S., Frigerio M., et al. Controlled gamma-ray irradiation of heparin generates oligosaccharides enriched in highly sulfated sequences Carbohydr Polym // Arzneimittelforschung.- 2004.- V.55.-№I.- P.10I-112.
- Bittl J.A., Chaitman B.R., Feit F., et al. Bivalirudin versus heparin during coronary angioplasty for unstable or post-infarction angina: the final report of the Bivalirudin Angioplasty Study. // Am Heart .1, — 2001 Dec.- V.142.- № 6, — P.952−961.
- Black M. The keratoses of the larynx // Proc R Soc Med.- 1954.- V.47.- №.4.- P.245−254.
- Blondin C., Chaubet F., Nardella A., et al. Relationships between chemical characteristics and anticomplementary activity of fucans // Biomaterials. 1996, — V. l7.- № 6.- P.597−603.
- Boisson-Vidal C., Haroun-Bouhedja F., Ellouali M., et al. Biological activities of polysaccharides from marine algae // Drugs of the Future, 1995.- V.20.- №.5.- P. 1237−1249.
- Boneu B. Low molecular weight heparins: Are they superior lo unfractionated heparins to prevent and to treat deep vein thrombosis? // Thromb Res. 2000.- VI00.- № 2, — P. 113−120.
- Boneu В., Caranobe C., Cadroy Y., et al. Pharmacokinetic studies of standard UFH, and low molecular weight heparins in the rabbit // Semin Thromb Hemost. 1988, — V. 14.- № 1.- P. 18−27.
- Bounameaux H., de Moerloose P. Is laboratory monitoring of low-molecular-weight heparin therapy necessary? No. // J Thromb Haemosl. 2004, — V.2.- № 2, — P.551 -555.
- Bradbrook I.D., Magnani H.N. Moelker H.C., et al. ORG 10 172: a low molecular weight heparinoid anticoagulant with a long half life in man // Br J Clin Pharmacol. 1987.- V.23.- № 6.-P.667−675.
- Bratl G., Tornebohm E., Widlund L. et al. Low molecular weight heparin (KABI 2165, FRAGMIN): pharmacokinetics after intravenous and subcutaneous administration in human volunteers//Thromb Res. 1986.- V.42.-№ 5,-P.613−620.
- Bray A.A.The evolution of the terrestrial vertebrates: environmental and physiological considerations //Trans R Soc Lond В Biol Sci. 1985.- V. 309.- № 1138, — P.289−322.
- Brian F., Gage M.D., Charles S. Pharmacogenetics and Anticoagulant Therapy // Journal of Thrombosis and Thrombolysis. 2003, — V.16.- №½.- P. 73−78.
- Brufatto N., Nesheim M.E. The use of prothrombin S525C) labeled with fluorescein to directly study the inhibition of prothrombinase by antithrombin during prothrombin activation // J Biol Chem. 2001.- V.276.- № 21.- P. 17 663−17 671.
- Buchanan M. R., Liao P. Smith L. J., and Ofusu F. A. Prevention of thrombus formation and growth by anti thrombin III and heparin cofactor Il-dependent thrombin inhibitors: impotance of heparin cofactor II //Thromb. Res. 1994, — V.74.- № 5.- P.463−475.
- Buchanan M.R., Blister S.J., Ofosu F. prevention and treatment of thrombosis novel strategies arising from our understanding the healthy endothelium // Wien. Klin. Wochenschr. 1993. V.105.- № 11.- P.309−313.
- Burgess J.K., Chong B.H. The platelet proaggregating and potentiating effects of unfractionated heparin, low molecular weight heparin and heparinoid in intensive care patients and healthy controls//Eur J Haematol. 1997, — V.58.-№ 4.- P.270−355.
- Bussel J.B., Steinherz P.G., Miller D.R. Hilgartner M.W. A heparin-like anticoagulant in an eight-month-old boy with acute monoblastic leukemia // Am J Hematol. 1984.- V.16.- № 1. P.83−90.
- Byun Y., Singh V.K., Yang V.C. Low Molecular Weight Protamine: A Potential Nontoxic Heparin Antagonist // Thrombosis Research 1999.- V.94.- № 1, — P.53−61.
- Cade J.F., Buchanan M.R., Boneu В. et al. A comparison of the antithrombotic and haemorrhagic effects of low molecular weight heparin fractions: the influence of the method of preparation // Thromb Res. 1984.- V.35.- № 6, — P.613−625.
- Calabrese G.C., Alberto M.F., Tubio R., et al. A small fraction of dermatan sulfate with significantly increased anticoagulant activity was selected by interaction with first complement protein.// Thromb. Res. 2004.- V. l 13.- № 3−4, — P.243−250.
- Capila I., Linhardt R. J. Hcparin-protein interactions // Angew. Chem. Int. Ed. 2002-V.41.- № 3, — P.390−412.
- Carr J.A., Silverman N., The heparin protamine interaction // J. Cardiovasc. Surg. 1999.-V.40.- № 3.- P.659−665.
- Carter C.J., Kelton J.G., Hirsh J., et al. The relationship between the hemorrhagic and antithrombotic properties of low molecular weight heparins in rabbits // Blood 1982.- V.59.- № 6.-P.1239−1245.
- Casati V., Guzzon D., Oppizzi M. et al. Hemostatic effects of aprotinin, tranexamic acid and ?-aminocaproic acid in primary cardiac surgery // Ann Thorac Surg 1999, — V.68.- № 1.- P.2252−2256.
- Casu B. Structure and biological activity of heparin // Adv. Carbohydr. Chem. Biochem. 1985, — №.43, — P.51−134.
- Casu В. Guerrini M., Naggi A., et al. Characterization of sulfation patterns of beef and pig mucosal heparins by nuclear magnetic resonance spectroscopy // Arzneimittelforshung. 1996.-V.46.-№ 5.- P.472−477.
- Casu В. Lindahl U. Structure and biological interactions of heparin and heparan sulfate // Adv. Carbohydr. Chem. Biochem. 2001.- № 57.- P. 159−206.
- Casu В., Guerrini M., Guglieri S., et al. Undersulfated and glycol-split heparins endowed with antiangiogenic activity // J. Med. Chem. 2004, — V.47.- № 4, — P. 838−848.
- Casu B. Structure and active domains of heparin // Elsevier Ltd. .- 2006.- V.399.- №.1.-P.l-28.
- Cetinel S., Ercan F., Sirvanci S., et al. The ameliorating effect of melatonin on protamine sulfate induced bladder injury and its lelationship to interstitial cystitis // J.Urol. 2003.- V.169.-№ 4,-P. 1564−1568.
- Chargaff E., Olson K.B.: Studies on the chemistry of blood coagulation. VI. Studies on the action of heparin and other anticoagulants. The influence of protamine on the anticoagulant effect in vivo // J Biol Chem. 1937.- V. 122, — № 1.- P. 153−167.
- Chavante S.F., Santos E.A., Oliveira F.W. A novel heparan sulphate with high degree of N-sulphation and high heparin cofactor-II activity from the brine shrimp artemia franciscana // Int.J.Biol.Macromol.2000.- V.27.- № 1.- P. 49−57.
- Chen W.H., Lau C.P., Lau Y.K., et al. Stable and Optimal Anticoagulation is Achieved With a Single Dose of Intravenous Enoxaparin in Patients Undeigoing Percutaneous Coronary Intervention // J Invasive Cardiol 2002, — V. 14 № 8, — P.439−442.
- Chevolot L., Foucault A., Chaubet F. et al Further data on the structure of brown seaweed fucans: relationships with anticoagulant activity // Carbohydr. Res. 1999.- V.319.- № 1−4, — P. 154 165.
- Chong B.H., Berndt M.C. Heparin-induced thrombocytopenia // Blut 1989, — V.58.- № 2.-P.53−60.
- Chong B.H., Ismail F. The mechanism of heparin-induced platelet aggregation // Eur J Haematol 1989,-V.43.-№ 3, — P.245−296.
- Cohen M. The role of low-molecular-weight heparins in arterial diseases: Optimizing antithrombotic therapy // Thromb Res. 2000, — V.100.- № 2, — P. 131- 139.
- Colliec S., Boisson-Vidal C., Jozefonvicz J. A low molecular weight fucoidan fraction from the brown seaweed Palvetia canaliculata //Phytochemistry 1994, — V.35.- № 3, — P. 697−700.
- Colucci M. Saidella L., Barbanti M" et al. Thrombolysis enhancing activity of a low molecular weight dermatan sulfate (Desmin 370) in experimental pulmonary embolism in rats // Thromb. Res. 1997, — V. 87, — № 5.- P. 441−146.
- Connolly S. J. Atrial Fibrillation Investigators. Risk factors for stroke and efficacy of antithrombotic therapy in atrial fibrillation // Arch Intern Med 1994, — V.154.- № 4.- P. 1449−1457.
- Conrad H. E. Heparin-Binding Proteins // Academic Press: San Diego. V.10.- № 2.- P. 137 141.- 1998.
- Coyne E. «Heparin past, present and future. In.: Chemistry and biology of heparin. Ed. Lundblad R.L., Brown W.V., Mann K.G., et al.» — New-York: EIsevier/North-Holland. 1981, — p.9−17.
- Crowther M.A. Berry L.R., Monagle P.T., Chan A.K.Mechanisms responsible for the failure of protamine to inactivate low-molecular-weight heparin // British Journal of Haematology, 2002, — V. l 16, — № 1, — P.178−186.
- Cumming A.M. Jones G.R., Wensley R.T., Cundall R.B.: In vitro neutralization of heparin in plasma prior to the activated partial thromboplastin time test: an assessment of four heparin // Thromb Res. 1986, — V.41.-№ 1.- P.43−56.
- D’Ambra M.N., Akins C.W. Blackstone E.H., et al. Aprotinin in primary valve replacement and reconstruction: a multicenter, double-blind, placebo-controlled trial // J Thorac Cardiovasci
- Surg. 1996, — V. l 12, — № 4.- P.1081−1090.
- Daud A.N., Ahsan A., Iqbal O., et al. Synthetic heparin pentasaccharide depolymerization by heparinase 1: molecular and biological implications // Clin. Appl. Thromb. Hemost. 2001,-V.7.- № 1.- P.58−64.
- Dehmer G. J., Fisher M., Tate D. A., et al. Reversal of Heparin Anticoagulation by Recombinant Platelet Factor 4 in Humans // Circulation, 1995, — V.91.- № 8, — P.2188−2194.
- Del Re M.R., Ayd J.D., Schultheis L.W. Heitmiller E.S., Protamine and left ventricular function: a transesophageal echocardiography study // Anesth. Analg. 1993, — V.77.- № 6.-P.1098−1103.
- Delorme M.A., Xu L., Berry L., et al. Anticoagulant dermatan sulfate proteoglycan (decorin) in the term human placenta // Tromb. Res. 1998.- V.90.- № 4.- P. 147−153.
- Demir M. Iqbal O., Hoppensteadt D.A., et al. Anticoagulant and antiprotease profiles of a novel natural heparinomimetic mannopentaose phosphate sulfate (PI-88) // Clin Appl Thromb Hemost. 2001.- V.7.- № 2, — P. 131 -171.
- Demirkan A., Mesut A., Aykut S., Kutlay N. Effect of Intraperitoneal Administration of Low-Moleculai-Weight Heparin on Plasma Tissue Factor Pathway Inhibitor Levels in CAPD Patients // Nephron.- 2002,-№ 91, — P. 162−163.
- Desai U. R. New Antithrombin-based anticoagulants // Med. Res. Rev. 2004, — V.24.- № 24.-P.151−181.
- Deux J.F., Meddahi-Pelle A., Le Blanche A.F., et al. Low Molecular Weight Fucoidan Prevents Neointimal Hyperplasia in Rabbit Iliac Artery In-Stent Restenosis Model. Letourneur Arterioscler // ThiombVasc Biol. 2002, — V.22.- № 10, — P.1604−1609.
- Dol F, Caranobe C, Dupouy D, Petitou M, et al. Effects of increased sulfation of dermatan sulfate on its in vitro and in vivo pharmacological properties // Thromb Res, 1988.- V52.- № 2.-P. 153−217.
- Douketis J.D., Foster G.A., Crowther M.A., et al. Clinical risk factors and timing of recurrent venous thromboembolism during the initial 3 months of anticoagulant therapy // Arch Intern Med 2000, — V. 160,-№ 22.- P.3431−3436.
- Doutremepuich С., Bonini F., Toulemonde F., et al. In vivo neutralization of low-molecular weight heparin fraction CY 216 by protamine // Semin Thromb Hemost. 1985.- V.ll.- № 3,-P.318−322.
- Drozd N.N., Sher A.I., Makarov V.A., et al. Comparison of antithrombin activity of the polysulphate chitosan derivatives in in vivo and in vitro system // Tromb. Res. 2001, — V.102.- № 5,-P.445−500.
- Dunaevsky Y. E., Gruban’T. N. Belyakova G. A., Belozersky M. A. Proteinase inhibitors in higher plants Hi. Plant Physiol. 1998.- V. 152, — № 6.- P.349−353
- Dyke C.K., Becker R.C., Kleiman N.S., et al. First experience with direct factor Xa inhibition in patients with stable coronary disease: a pharmacokinetic and pharmacodynamic evaluation // Circulation. 2002, — V.105.- № 20, — P.2385−2391.
- Edens R. E., Al-Hakim A., Weiler J. M. et al Gradient Polyacrylamide Gel Electrophoresis for Determination of the Molecular Weights offleparin Preparations and Low-Molecular-Weight Heparin Derivatives // J. Pharm. Sci. 1992, — V.81.- № 8, — P.823−827.
- Edward В., Braun, Karen L., et al. Intraoperative Use of Aminocaproic Acid in Liver // Transplant RecipientsAnesthesiology 2006.- V.105.-№ 3.- P. 1685.
- Edwards J.O., Curci R. Fenton type activation and chemistry of hydroxyl radical. In: Strukul G ed. Catalytic Oxidations with Hydrogen Peroxide as Oxidant // London: Kluwer Academic. 1992, — P.97−153.
- Eikelboom J.W., Quinlan D.J., Douketis J.D. Extended-duration prophylaxis against VTE after total hip or knee replacement: a meta-analysis ofthe randomised trials // Lancet. 2001.-V.358.- № 9275.- P.9−15.
- Esko J. D. Xindahl U. Molecular diversity of heparan sulfate // J. Clin. Invest. 2001.-V.108.- № 2, — P.169−173.
- Esmon CT. The protein С pathway.// Chest 2003. V.124.- S.3.- P.26S-32S.
- European Pharmacopoeia, 5th edition published 15.6.2004, valid from 1.1.2005
- Fabian I, Aronson M. Polycations as possible substitutes for protamine in heparin neutralization//Thromb Res. 1980.- V.17.-№ 1−2.-P.239−247.
- Fareed J., Fu K., Yang L.H., et al. Pharmacokinetics of low molecular weight heparins in animal models // Semin Thromb Hemost 1999.- V.25.- S.3.- P.51 -55.
- Farias W.R.L. Valente A-P., Pereira M.S., Mourao P.A.S. Structure and Anticoagulant Activity of Sulfated Galactans.// J. Biol. Chem., 2000.- V. 275.- №.38, — P.29 299−29 307.
- Ferguson J.J. Meeting highlights В American Heart Association scientific sessions 2001 // Circulation 2002, — V106.- № 7,-P.e24-e30.
- Fernarndez C., Hattan C.M., Kerns R.J. Semi-synthetic heparin derivatives: chemical modifications of heparin beyond chain length, sulfate substitution pattern and N-sulfo/N-acetyl groups//Carbohydrate Research. 2006.- V.341.- № 10.-P.1253−1265.
- Fiore M. M., Kakkar V. V. Platelet factor 4 (PF4) neutralizes heparan sulfate-dependent inactivation of factor Xa by preventing enzyme interaction with polysaccharide //Biochem Biophys Res Commun. 2003.- V.311.- № 1.- P.71−76.
- Fischer A. Die Bindung von Heparin an Eiweiss // Biochem Zeit. 1935, — P. 278−133
- Francis C.W., Davidson B.L., Berkovvitz S.D., et al. Ximelagatran versus warfarin for the prevention of venous thromboembolism after total knee arthroplasty. A randomized, double-blind trial // Ann Intern Med. 2002, — V. 137, — № 8. P.648−655.
- Frydman A. Bara L., Leroux Y." et al. The antithrombotic activity and pharmacokinetics of Enoxaparin. a low molecular weight heparin, in man given single subcutaneous doses of 20 up to 80 mg//J Clin Pharmacol. 1988.- V.28.-№ 1.- P.609−618.
- Fugedi P. The potential of the molecular diversity of heparin and heparan sulfate for drug development // Mini Rev. Med. Chem. 2003.- V.3.- № 7. P.659−667.
- Gage B.F., Cardinalli А.В., Albers G.W., Owens D. Costeffectiveness of warfarin and aspirin for prophylaxis of stroke in patients with nonvalvular atrial fibrillation // Stroke, 1998.-V.29.- № 6 P. 1083−1174.
- Ghosh R., Cui Z.F. Purification of lysozyme using ultrafiltration // Biotechnol Bioeng, 2000, — V.68.- № 2, — P.191−203.
- Giraux J.L., Tapon-Bretaudiere J., Matou S., Fischer A.M. Fucoidan, as heparin, induces tissue factor pathway inhibitor release from cultuied human endothelial cells // Thromb Haemost. 1998, — V.80.- № 4, — P.692−697.
- Godal H C. A comparison of two heparin-neutralizing agents: protamine and polybrene // Scan J Clin Lab Invest, I960, — №.12, — P.446−457.
- Gorog D.A., Alamgir Mn K., Michael S Marbcr. Role of LMWH in ACS, with or without PCI and GP Ilb/IIIa blockade // Br J Cardiol, 2004, — V. 11.- № 2, — P. AIC45-AIC52.
- Grabovac V., Schmitz Т., Foger F., Bernkop-Schniuch A. Papain: an effective permeation enhancer for orally administered low molecular weight heparin // Pharm Res. 2007, — V.24.- № 5.-P.1001−1007.
- Grauffel V., Kloareg В. Mabeau S. et al. New natural polysaccharides with potent antithrombic activity: fucans from brown algae // Biomaterials, 1989.- V. 10, — № 6, — P.363−371.
- Greinacher A. Volpel H, Janssens U, et al. Recombinant hirudin (lepirudin) provides safe and effective anticoagulation in patients with heparininduced thrombocytopenia: a prospective study // Circulation, 1999, — V.99.- № 1, — P.73−80.
- Griffin С. C., Linhardt R. J., VanGorp C. L., et al. Isolation and characterization of heparan sulfate from crude porcine intestinal mucosa peptidoglycan heparin // Carbohydr. Res. 1995,-V.276.- № 1.- P.183−197.
- Griffith M.J. Heparin-catalyzed inhibitor/protease reactions: kinetic evidence for a common mechanism of action of heparin // Proc Natl Acad Sci USA. 1983, — V.80.- № 18, — P.5460−5464.
- Gunay N.S. Linhardt R.J. Heparinoids: structure, biological activities and therapeutic applications //Planta Med. 1999, — V.65.- № 4, — P.301−306.
- Gustalsson D. Nystrom J.E., Carlsson S., et al. The direct thrombin inhibitor melagatran and its oral piodrug H 376/95: intestinal absorption properties, biochemical and pharmacodynamic effccts // Thromb Res. 2001.- V. 101.- № 3P. 171 -181
- Handoll H.H., Farrar M.J. McBiinie J., et al. Heparin, low molecular weight heparin and physical methods for preventing deep vein thrombosis and pulmonary embolism following surgery for hip fractures // Thromb Haemost., 1998, — V.79.- № 1, — P.902−906.
- Harenberg J. Pharmacology of low molecular weight heparins // Semin Thromb H 1990.- V.16.- № 12.- P.18.
- Harenberg J., Gnasso A., de Vries J.X. et al. J. Inhibition of low molecular weight h< by protamine chloride in vivo // Thromb Res., 1985, — V.38.- № 1.- P. 11- 20.
- Haroun-Bouhedja F., Ellouali M. Sinquin C. Boisson-Vidal C. Relationship b sulfate groups and biological activities of fucans // Thromb Res. 2000.- V.100.- № 5.- P.453−4parinveen
- Hayakawa Y., Hayashi Т., Lee J., et al. Inhibition of thrombin by sulfated polysacc^-^ isolated from green algae // Biochim.Biophys.Acta. 2000.- V. 1543, — № 1.- P.86−94.
- Herault J.P., Cappelle M., Bernat A., et al. Effect of SanOrg 12 3781A, a s.1.:hetichexadecasaccharide, on clot-bound thrombin and factor Xa in vitro and in vivo // J Thromb 2003, — V.I.- № 9.- P. 1959−1965.
- Hickey A.M., Marie L., McCreedy Т. et al. Immobilization of thermophilic enz^^es inminiaturized flow reactors // Biochem Soc Trans. 2007, — V.35.- № 6, — P. 1621−1624.
- Hirsh J., Levine M.N. Low molecular weight heparin // Blood 1992, — V.79.- № 1.- P17.
- Hirsh J., Warkentin Т.Е., Raschke R., et al. Heparin and low-molecular-weight1. Parin: ety //
- Mechanisms of action, pharmacokinetics, dosing considerations, monitoring, efficacy and ^ Chest 1998.- V. l 14.- S.5.- P.489S-510S.
- Hirsh J. Current anticoagulant therapy—unmet clinical needs // Thromb Res. 20 031. V-15.1, — P.1−8.
- Hirsh J., Raschke R. Heparin and Low-Molecular-Weight Heparin// Chest, 2004−126,1. S.3.- P.188S-203S.
- Hirsh J., O’Donnell M., and Weitz J. 1. New anticoagulants // Blood, 2005.- V. Jq^ P. 453−463.
- Holmer E., Mattsson C., Nilsson S. Anticoagulant and antithrombotic effects of heparin and low molccular weight heparin fragments in rabbits // Thromb Res. 1982 V.25.- № 2.- P.475- 485.
- Holmer E., Soderberg K,. Bergqvist D. et al. Heparin and its low molecular weight derivatives: anticoagulant and antithrombotic properties // Haemostasis 1986.- V.16.- S.2.- P. 1—7.
- Holzheimer R.G. Low-molecular-weight heparin (LMWH) in the treatment of thrombosis // Eur J Med Res. 2004, — V.30.- № 4, — P.225−264.
- Hongo R.H., Ley J., Dick S.E., Yee R.R. The effect of clopidogrel in combination with aspirin when given before coronary artery bypass grafting // J Am Coll Cardiol 2002, — V.40.- № 2,-P.231−238.
- Hoppensteadt D.A., Jeske W" Ahsan A., et al. Biochemical and pharmacologic profile of defined molecular weight fractions of heparin // Semin Thromb Hemost 1993.- V. 19.- S.I.- P.12−19.
- Hoppensteadt D.A., Iqbal 0., Fareed J. Basic and clinical differences of heparin and low molecular weight heparin treatment. In: Garg HG, Linhardt RJ, Hales CA eds. Chemistry and Biology of Heparin and Heparan Sulfate. Elsevier Ltd, 2006.- P.583−606.
- Home A., Gettins P. IHNMRspectroscopic studies on the interaction between human plasma antithrombin 111 and defined low moleculai weight heparin fragments // Biochemistry 1992, — V.31.- № 8.- P.2286−2294.
- Horrow J.C., Protamine: a review of its toxicity // Anesth. Analg. 1985, — V.64.- № 3, — P.348−361.
- Horstadius S., Lorch I.J., Chargaff E. The effect of deoxyribonucleic acids extracted from sea urchin sperm on the development of sea urchin eggs // Exp Cell Res. 1954, — V6.- № 2, — P.440−492.
- Hoylaerts M., Rijken D.C., Lijnen H.R., Collen D. Kinetics of the activation of plasminogen by human tissue plasminogen activator. Role of fibrin // J Biol Chem 1982, — V.257.-№ 6.- P.2912—2921.
- Huang R., Du Y., Yang J. Preparation and anticoagulant activity of carboxybutyrylated hydroxyethyl chitosan sulfates // Carbohydrate polymers 2003.- V.51.- № 4.- P.431−438.
- Huang R., Du Y., Yang J., Fan L Influence of functional groups on the in vitro anticoagulant activity of chitosan sulfate // Carbohydr Res. 2003, — V.338.- № 6.- P.483−492.
- Hubbard A.R., Jennings A. Neutralisation of heparan sulphate and low molecular weight heparin by protamine // Thromb Haemost 1985, — V.53.- № 1, — P.86- 95.
- Hulin M.S., T.W. Wakefield P.C. Andrews, S.K. et al. A novel protamine variant reversal of heparin anticoagulation in human blood in vitro // J. Vase. Surg. 1997.- V.26.- № 6.-P.1043−1048.
- Hulin MS, Wakefield TW, Andrews PC, et al. Comparison of the hemodynamic and hematologic toxicity of a protamine variant alter reversal of low-molecular-weight heparin anticoagulation in a canine model // Lab Animal Sci., 1997.- V.47.- № 2.- P. 153−60.
- Hurlen M., Abdelnoor M. Smith P. et al. Warfarin, aspirin, or both alter myocardial infarction // N Engl J Med. 2002, — V.347.- № 13.- P.969−974.
- Hursting M.J. Alford K.L., Becker J.C. et al. Novastan (biand of argatroban): a small-molecule, direct thrombin inhibitor // Semm Thromb Haemost. 1997.- V.23.- № 6, — P.503−516.
- Il’ina A.V., Varlamov V.P. Enzymatic depolymerization of N-succinylchitosan // Bioorg Khim. 2007.- V33.- № 1.- P. 156−165.
- Ishihara M., Ono K. Structure and function of heparin and heparan sulfate: heparinoid library and modification of FGF-activities // Trends Glycosci Glycotechnol. 1998.- V.10.- № 1.-P.223−233.
- Ishiquro K., Ohira Y., Oku H. Preventive effects of Impatiens balsamina on the hen egg-white lysozyme (HEL)-induced decrease in blood flow // Biol. Pharm. Bull. 2002.- V.25.- № 4,-P.505−513.
- Islam Т. Butler M. Sikkander S. A., et al. Further evidence that periodate cleavage of heparin occurs primarily through the antithrombin binding site // Carbohydr. Res. 2002, — V.337.-№ 21−23.-P.2239- 2243.
- Janes K. J., Fresneau M. P., Marazuela A., et al. Chitosan nanopartieles as delivery systems for doxorubicin // J Cont Rel., 2001.- V.73.- № 2−3, — P.255−267.
- Jenniskens G.J., Oosterhof A., Brandwijk R., et al. Heparan sulfate heterogeneity in skeletal muscle basal lamina: demonstration by phage display-derived antibodies // J Neurosci. 2000.-V.20.- № 11.- P.4099−4111.
- Ji H., Li S. P., Cheng X., et al. Antithrombotic effects of low-molecular-weight heparin calcium (LMWH-Ca) in experimental models // General Pharmacology 1999.- V.33.- № 2, — P.207−211.
- Johnson E.A., Kirkwood T.B., Stirling Y., et al. Four heparin preparations: anti-Xa potentiating effect of heparin after subcutaneous injection // Thromb Haemost 1976.- V.35.- № 3,-P.586−591.
- Johnson E.A., Mulloy B. The molecular weight range of commeicial heparin preparations // Carbohydr Res., 1976.- V.51.-№ 1- P. 119−127.
- Johnson P. H" HIRUDIN: Clinical Potential of a Thrombin Inhibitor // Annual Review of Medicine 1994, — V.45.- № 1.- P. 165−177.
- Jones G.R. Hashim R., Power D.M. A comparison of the strength of binding of antithrombin III, protamine and poly (L-lysine) to heparin samples of different anticoagulant activities // Biochimica Biophysica Acta 1986.- V.883.- № 1.- P.69−76.
- Jordan R.E., Oosta G.M. Gardner W.T., et al. The kinetics of hemostatic enzyme-antithrombin interactions in the presence of low molecular weight heparin // J Biol Chem 1980. V.255.- № 21, — P.10 081−10 090.
- Karkouti K., Beattie W.S. Aprotinin is useful as a hemostatic agent in cardiopulmonary surgery: no // Thromb Haemost, 2006, — V.4.- № 9.- P. 1879−1881
- Karst N. A., Linhardt R. J. Recent chemical and enzymatic approaches to the synthesis of glycosaminoglycan oligosaccharides. //Curr. Med. Chem. 2003.- V.10.- № 19.- P. 1993−2031.
- Kaufman P.Л., Gockerman J.P., Gieenberg C.S. Production of a novel anticoagulant by neoplastic plasma cells: report of a case and review of the literature // Am J Med 1989.- V.86.-№ 5.- P.612−616
- Kennedy C.C., Rocks W.J. Bedside control of heparin therapy simple whole blood clotting method// J Clin Phatol, 1973, — V.26.- № 11.- P.897−894.
- Khoory M.S., Nesheim M.E., Bowie E.J. Mann K.G. Circulating heparan sulfate proteoglycan anticoagulant from a patient with a plasma cell disorder // J Clin Invest 1980, — V.65.-№ 3, — P.666−674.
- Kifune K. In in «The developm’ent and application of chitin and chitosan», Industrial Technology Assotiation, Tokyo, 1987, — P.233.
- Kindlei C., A. Bircher, P. Stulz, Protamine-induced fulminant noncardiogenic pulmonary edema following cardiopulmonary bypass // Eur. J. Cardiothorac. Surg. 1996.- V.10.- № 6.-P.463— 466.
- Kjellen L" Lindahl U. Proteoglycans: structures and interactions // Ann Rev Biochern. 1991.- V.60.-№ 1.- P.443−475.
- Kuberan В., Beeler D. L., Lech M., et al. Chemoenzymatic synthesis of classical and non-classical anticoagulant heparan sulfate polysaccharides // J. Biol. Chem. 2003.- V.278.-№ 352.- p. 52 613−52 621.
- Kumada Т., Abiko Y. Fibrinolytic action of a new semi-synthetic polysaccharide sulfate, galactan polysulfate (DH6322), in the rat // Thromb Res 1985.- V.39.- № 1.- P.9−19.
- Kumar M. N. A review of chitin and chitosan applications, React Funct Polym // J Am Chem Soc. 2005, — V.127.- № 22, — P.8204−8217.
- Kurtz A.B., Gray R.S. Markanday S., Nabarro J.D. Circulating IgG antibody to protamine in patients treated with protamine-insulins // Diabetologia 1983.- V.25.- № 4, — P.322−324.
- Kyogashima M. Onaya J" Miyauchi S., et al. Antitrombotic activity of avian crown dermatan sulfate.//Tromb. Res. 1999.- V.9,6.- № 6.- P.459−465.
- Lane D.A., Denton J. Flynn A.M., et al. Anticoagulant activities of heparin oligosaccharides and their neutralization by platelet factor 4 // Biochem J., 1984, — V.218.- № 3.-P.725−732.
- Lauient T.C., Tengblad A., Thunberg L., et al. The molecular-weight-dependence of the anti-coagulant activity of heparin // Biochem J. 1978.- V.175.- № 2.- P.691−701.
- Lee J. Y., Nam S. H., Im S. Y. et al. Enhanced bone formation by controlled giowth factor delivery from chitosan-based biomaterials // J Cont Rel, 2002.- V.78.- № 1−3, — P. 187−197.
- Lee R.I., White P.D. A clinical study of the coagulation time of blood // Am J Med Science, 1913.-№.145,-P.495−503.
- Lemmer Jr. J.H., Dilling E.W. Morton J.R., et al. Aprotinin for primary coronary artery bypass grafting: a multicenter trial of three dose regimens // Ann Thorac Surg 1996.- V.62.- № 2,-P. 1659−1726.
- Lever R., Page C. P., Novel drug development opportunities for heparin // Nat. Rev Drug Discov. 2002.- V.I.- № 2, — P.140−148.
- Levine M. N., Raskob G., Landefeld S., Kearon C. Hemorrhagic complications of anticoagulant treatment // Chest 2001.- V. 119, — № 1.- P. 108S-121S.
- Levine M.N., Hirsh J., Gent M., et al. A randomized trial comparing activated thromboplastin time with heparin assay in patients with acute venous thromboembolism requiring large daily doses of heparin // Arch Intern Med. 1994.- V.154.- № 1.- P.49−56.
- Levy J.H., Bailey J.M., Salmenpera M. Pharmacokinetics of aprotinin in preoperative cardiac surgical patients//Anesthesiology 1994, — V.80.-№ 5.- P. 1013−1021.
- Levy J.H., Cormack J.G., Morales A. Heparin neutralization by recombinant platelet factor 4 and protamine // Anesih. Analg. 1995.- V.81№ 1.- P.35−37.
- Levy J.H., Ramsay J.G., Guyton R.A. Aprotinin in cardiac surgery // N Engl J Med 2006.-V.354.- № 4.- P.1953−1960.
- Lin P., Sinha U. Betz A. Antithrombin binding of lowmolecular weight heparins and inhibition of factor Xa//Biochim Biophys Acta 2001.- V.1526.-№ 1.- P. 105−113.
- Lindblad В., Borgstrom A., Wakefield T.W., et al. Protamine reversal of anticoagulation acheived with a low molecular weight heparin. The effect on eicosanoids, clotting and complement factors // Thromb Res 1987, — V.48.- № 1, — P.31−40.
- Lindblad В., Prolamine sulphate: a review of its effects: hypersensitivity and toxicity // Eur. J. Vase. Surg. 1989, — V.3.- № 3, — P. 195−201.240., Linhardt R. J., Galliher P. M., Cooney C. L. Polysaccharide lyases // Appl. Biochem. j |
- Biotechnol. 1986, — V. 12, — № 2, — P. 135−176,i
- Linhardt R. J., Rice K. G., Kim Y. S., et al. Mapping and quantification of the major oligosaccharide components of heparin // Biochem. J. 1988.- V.254.- № 3, — P.781−787.
- Linhardt R. J. Heparin: an important drug enters its seventh decade // Chem. Ind. 1991.-V.2.- № 1.- P.45−50.
- Linhardt R. J., Toida T. «Heparin oligosaccharides: new analogues development and applications. In Carbohydrates in Drug Design» Witczak Z. J., Nieforth K. A. Marcel Dekker: New York, 1997.- Ch.7.- P.277−341.
- Linhardt R. J., Gunay N. S. Production and Chemical Processing of Low Molecular Weight Heparins // Semin. Thromb. Hemostasis 1999, — V.25.- № 3, — P.5−16.
- Linhardt, R. J. Heparin: structure and activity // J. Med. Chem. 2003, — V.46.- № 1.- P.2551−2564.
- Linhardt R.J., Toida T.T. Role of glycosaminoglycans in cellular communication // Acc. Chem. Res. 2004, — V.37.- № 7, — P.431138.
- Liu J., Thorp S. C. Cell surface heparan sulfate and its roles in assisting viral infections // Med. Res. Rev. 2002,-V.22.-№ 1.- P. 1−25.
- Llamas P., OuteirhTo J., Espinoza J., et al. Report of three cases of circulating heparin-like anticoagulants // Am J Hematol 2001.- V.67.- № 4.- P.256−258.
- Loganathan D., Wang H. M., Mallis L. M., Linhardt R. J. Structural variation in the antithrombin III binding site region and its occurrence in heparin from different sources // Biochemistry 1990.- V.29.- № 18, — P.4362−4368.
- Logeart-Avramoglou D., Josefonvicz J. Carboxymethyl benzylamide sulfonate dextrans (CMDBS), a family of biospecific polymers endowed with numerous biological properties: A review // J. Biomed. Mater. Res. 1999, — V.48.- № 4, — P.578−590.
- Lohse D. L., Linhardt R. J. Purification and characterization of heparin lyases from Flavobacterium heparinum // J. Biol. Chem. 1992, — V.267.- № 34.- P.24 347−24 355.
- Lonneau J.C., Herault J.P. Compaiative inhibition of extrinsic and intrinsic thrombin generation by standard heparin, a low molecular weight heparin and the synthetic ATIII-binding pentasaccharide//Thromb Haemost 1993.- V69.-№ 2.- P. 152.
- Lowary L. R., Smith F. A., Coyne E., Dunham N. W. Comparative neutralization of lung-and mucosal-derived heparin by prolamine sulfate using in vitro and in vivo methods // Journal of Pharmaceutical Sciences 1970, — V.60.- № 4, — P.638−640.
- Lowry O.H., Rosebrough N.J., Farr A.L., Randall R.J. Protein measurement with the folin phenol reagent// J Biol Chem 1951, — V.193.- № 1 P.265−340.
- Lubenow N., Kempf R., Eichner A., et al. Heparin-induced thrombocytopenia: temporal pattern of thrombocytopenia in relation to initial use or reexposure to heparin // Chest. 2002,-V.122.- № 1 P.37−42.
- Ma Q., Tobu M, Schultz C., et al. Molecular weight dependent tissue factor pathway inhibitor lelease by heparin and heparin oligosaccharides // Thrombosis Research 2007.- V.119.-№.5, — P.- 63−661.
- Maccarana M., Sakura Y., Tawada A., et al. Domain structure of heparan sulfates from bovine org ms // J Biol Chem 1996, — V.271.- № 30, — P. 17 804−17 810.
- Magnani A., Albanese A, Lamponi S, Barbucci R. Blood-interaction performance of defferently sulphated hyaluronic acids//Thrombosis Res, 1996.- V. 81.- № 3.-P.383−395.
- Malleier J., Oskolkova O., Bochkov V., et al. Phosphatidylserine and oxidized phosphatidylethanolamine interact with Protein С Inhibitor (PCI) and modify its activity // Journal of Thrombosis and Haemostasis, 2006.- V.4.- № 1, — P.199−199.
- Markwardt F., Klocking H.P. Heparin-induced release of plasminogen activator // Haemostasis 1977, — V.6.- № 6, — P.370−374.
- Maruyama H.B., Suhara Y., Suzuki-Watanabe J., et al. A new antibiotic, fumaramidmycin I. Production, biological properties and characterization of producer strain // J Antibiot (Tokyo). 1975, — V.28.- № 9.- P.636−47.
- Masuda K.H., Kyogashima M., Ishii T. Isolation and partial characterization of fucan sulfates from the body wall of sea cucumber Stichopus japonicus and their ability to inhibit osteoclastogenesis // Carbohydr. Res. 2004, — V.339.- № 7.- P.1339−1346.
- Mateo C, Grazu V, Pessela ВС, et al. Advances in the design of new epoxy supports for enzyme immobilization-stabilization // Biochem Soc Trans. 2007, — V.35.- № 6.- P.1593−601.
- Matsuo Т., Shanberge J.N., Matsuo О. Effect of protamine sulphate on antithrombin III activity// Clin Chim Acta 1983.- V.131.- № 3, — P.233−238.
- Matthiasson S.E., Lindblad В., Stjernquist U., Bergqvist D. The Haemorragic effect of low molecular weight heparins, dermatan sulphate and hirudin // Haemostasis 1995.- V.25.- № 5.-P.203−211.
- Mattsson C., Palm M., Soderberg K., Holmer E. Antitrombotic effects of heparin oligosaccharides//Ann. N. Y. Acad. Sci., 1989.-V.556.-№ 1.- P.323−32.
- Matzsch Т., Bergqvist D., Hedner U., et al. Effect of an enzymatically depolymerized heparin as compared with conventional heparin in healthy volunteers // Thromb Haemost 1987.-V.57.- № 1.- P.97−101.
- Mauray S., De Raucourt E., Chaubet F., et al. Comparative anticoagulant activity and influence on thrombin generation of dextran derivatives and of a fucoidan fraction // J Biomater Sci Polym Ed., 1998, — V.9.- № 4, — P.373−460.
- McEvoy G.K. American Hospital Formulary Service Drug Information 1998 // American Society of Health-System Pharmacists, 1998.- V.33.- № 6.- P.611−612.
- Melo F.R., Pereira M.S., Foguel D., Mourao P.A. Antithrombin-mediated anticoagulant activity of sulfated polysaccharides: different mechanisms for heparin and sulfated galactans // J. Biol. Chem. 2004, — V.279.- № 20, — P.20 824−20 859.
- Messmore H. L., Wehrmacher W. H., Coyne E., Fareed J. Heparin to pentasaccharide and beyond: the end is not in sight // Semin. Thromb. Hemost. 2004, — V.30.- № 1, — P.81−88.
- Mestechkina N. M., Shcherbukhin V. D., Bannikova G. E., et al. Anticoagulant activity of low-molecular-weight sulfated derivatives of galactomannan from Cyamopsis tetragonoloba (L.) seeds // Prikl Biokhim Mikrobiol. 2008, — V.44.- № 1.- P. 111 -117
- Mikola J., Suolinna E. Purification and properties of an inhibitor of microbial alkaline proteinases from barley // Arch. Biochem. Biophys. 1971.- V. l44, — № 2.- P.566−575.
- Mine Y., Ma F., Lauriau S. J. Antimicrobial peptides released by enzymatic hydrolysis of hen egg white lysozyme // Agric Food Chem. 2004, — V.52.-№ 5.- 1088−2030.
- Minix R., Doctor V. Interaction of fucoidan with proteases and inhibitors of coagulation and fibrinolysis // Tromb. Res. 1997, — V.87.- № 1.- P.419−429.
- Mitchell M. A., Wilks J. W. Inhibitors, of angiogenesis Academic Press: San Diego, 1992.-V. 27.
- Mochizuki Т., Olson P.J., Szlam F., et al. Protamine reversal of heparin affects platelet aggregation and activated clotting time after cardiopulmonary bypass // Anesth Analgesia 1998,-V.87.- № 4, — P.781−786.
- Mohammad S. F., Anderson W. H., Smith J. В., Chuang H. Y. Effects of heparin on platelet aggregation and release and thromboxane A2 production. and R. G. Mason // Am J Pathol. 198.- 1,-V.104.- № 2, — P.132—141.
- Moll S., Lindley C., Pescatore S., et al. Phase 1 study of a novel recombinant human soluble thrombomodulin ART-123 // J Thromb Haemost. 2004, — V.2.- № 10, — P. 1745−1796.
- Monien B.H., Henry B.L., Raghuraman A., et al Novel chemo-enzymatic oligomers of cinnamic acids as direct and indirect inhibitors of coagulation proteinases // Bioorg Med Chem. 2006.- V. 14, — № 23.- P.7988−7998.
- Mosolov V. V., Sokolova E.V., Livenskaya O. A. Spectra of circular dichroism of proteinase inhibitors from corn// Biokhimiya 1983.- V.48.- № 9, — P.1538−1579.
- Mosolov V.V., Grigor’eva L.I., Valueva T.A. The role of proteolytic enzymes and their inhibitors in plant protection (review) // Prikl Biokhim Mikrobiol. 2001.- V.37.- № 2, — P.131−171.
- Mosolov V.V., Valueva T.A. Participation of proteolytic enzymes in the interaction of plants with phytopathogenic microorganisms // Biochemistry (Mosc). 2006.- V.71.- № 8.- P.838−883.
- Motulsky H.J., Cristopoulos A. «Fitting Models to Biological Data using Linear and Nonlinear Regression» GraphPad Software Inc, San Diego С A, 2003.
- Mourao P.A., Pereira M.S. Searching for alternatives to heparin. Sulfated fucan from marine invertrbrates // Trends Cardiovasc.Med. 1999.- V.9.- № 8.- P.225−232.
- Mousa S., Fareed J. Overview: from heparin to low molecular weight heparins: beyond anticoagulation// Curr Opin Invest Drug 2001.- V.2.- № 8.- P. 1077−1080.
- Muzzarelli R., in «Advances in chitin and chitosan «(Eds Brine C.J., Sndoford PA, Zikakis JP), Elsevier Applied Science, London and New-York, 1992.- P.-25
- Myllymaki O., Eerikainen Т., Suortti Т., et al. Depolymerization of Barley Starch during Extrusion in Water Glycerol Mixtures // Lebensmittel-Wissenschaft und-Technologie 1997.- V.30.-№ 4.- P.351−358.
- Nader H. В., Dietrich C. P. Natural occurrence and possible biological role of heparin. In Heparin Chemical and Biological Properties, Clinical Applications- Lane D. A., Lindahl U., Eds.- CRC Press: Boca Raton, FL, 1989.- P. 115−133.
- Nader H.B., Lopes C. C, Rocha H.A., et al. Heparins and heparinoids: occurrence, structure and mechanism of antithrombotic and hemorrhagic activities // Curr. Pharm. Des.2004.- V.10.-№ 9.- P.951−966.
- Naggi A., Casu В., Perez M., et al Modulation of the heparanase-inhibiting activity of heparin through selective desulfation, graded N-acetylation, and glycol splitting // J. Biol. Chem. 2005.- V.280.- № 13.- P. 12 103−12 113. «
- Nishino Т., Yamauchi Т., Horie M., et al. Effects of a fucoidan on the activation of plasminogen by u-PA and t-PA // Thromb Res. 2000.- V.99.- № 6.- P.623−659.
- Ockelford P. A, Carter C.J., Cerskus A., et al. Comparison of the in vivo hemorrhagic andvantithrombotic effects of a low antithrombin-III affinity heparin fraction // Thromb Res 1982.-V.27.- № 1.- P.679−690.
- Ofosu F. A., Modi G. J., Blajchman M. A., et al. Increased sulphation improves the anticoagulant activities of heparan sulphate and dermatan sulphate // Biochem J. 1987.- V.15.-№ 248, — P. 889−896.
- Ofosu A., Gray E. Mechanisms of action of heparin: applications to the development of derivatives of heparin and heparinoids with antithrombotic properties // Sem Thromb Haem, 1988,-V.14.- № 1.- P.9−15.
- Okajima Y., Kanayama S., Maeda Y., et al. Studies on the neutralizing mechanism of antithrombin activity of heparin by protamine // Thromb. Res. 1981, — V.24.- № 2, — P.21−29.
- Oku K., Kawamura Y., Nakade H., et al. Heparin-induced aggregation is recognized on platelets activated by physical stimuli // Japanese Journal of Medical Technology 2003.- V.52.-№ 12, — P.1431−1435.
- O’Leary R., Rerek M., Wood E. Fucoidan modulates the effect of transforming growth factor (TGF)-betal on fibroblast proliferation and wound repopulation in in vitro models of dermal wound repair // J. Biol Pharm Bull. 2004, — V.27.- № 2 .- P266−336.
- Otakara A., in «The development and application of chitin and chitosan», Industrial Technology Assotiation, Tokyo, 1987.- P.161.
- Padilla A., Gray E., Duncan S. et al. Inhibition of thrombin generation by heparin and low molecular weight (LMW) heparins in the absence and presence of platelet factor 4 (PF4) // British Journal of Haematology 2008, — V. 82, — № 2, — P.406 413.
- Palm M., Mattsson C. Pharmacokinetics of heparin and low molecular weight heparin fragment (Fragmin) in rabbits with impaired renal or metabolic clearance // Thromb Res 1985.-V.40.-№ 1.- P. 129−133.
- Palmer R.N., Rich M.E., Rick P.D., et al. Circulating heparin sulfate anticoagulant in a patient with a fatal bleeding disorder // N Engl J Med 1984, — V.310.- № 7, — P. 1696−1699.
- Paques E.P., Stohr H.A., Pleimburger N. Study on the mechanism of action of heparin and related substances on the fibrinolytic system: relationship between plasminogen activators and heparin // Thromb Res 1986.-V.42, — № 2, — P.797−807.
- Pavao M.S.G., Aiello K.R.M., Wemeck C.C., et al. Higly sulfated dermatan sulfates from Ascidians // J.Biol.Chem. 1998, — V.273.- № 43.- P.27 848−27 857.
- Pejler G., Danielsson A., Bjork I., et al. Structure and antithrombin binding properties of heparin isolated from the clams Anomalocardia brasiliana and Tivela macroides // J Biol Chem 1987, — V.262.- № 17, — P. l 1413−11 421.
- Pellegrini A., Thomas U., Bramas N. et al. Identification and isolation of a bactericidal domain in chicken egg white lysozyme // Appl. Microbiol. 1997.- V.82.- № 3, — P.372−380.
- Pereira M.S., Mulloy В., Mourao P.A.S. Structure and anticoagulant activity of sulfated fucans // J.Biol.Chem. 1999, — V.274.- № 43, — P.7656−7667.
- Pereira M.S., Melo F.R., Mourao P.A. Is there a correlation between structure and anticoagulant action of sulfated galactans and sulfated fucans? // Glycobiology 2002, — V.12.-№ 10.- P.573−580.
- Pervin A., Gallo C., Jandik К A., et al. Preparation and structural charactcrization of large heparinderived oligosaccharides // Glycobiology 1995.- V.5.- № 1, — P.83−95.
- Petitou M., Herault J.P., Bernat A., et al. Synthesis of Ihrombin-inhibiting heparin mimelics without side effects //Nature.1999.- V.398.- № 6726, — P.417−422.
- Petitou M., Imberty A., Duchaussoy P., et al. Experimental proof for the structure of a thrombin-inhibiting heparin molecule // Chemistry. 2001, — V.7.- № 1.- P.858−931.
- Pires L., Gorin P.A.J., Reicher F., Sierakowski M. R. An active heparinoid obtained by sulphation of a galactomannan extracted from the endosperm of Senna macranthra seeds // Caibohydr. Res 2001.- V.46.- № 2, — P.165−169.
- Pletcher C.H., Nelsestuen G.L. Two-substrate reaction models for the heparin-catalyzed bovine antithrombin/protease reaction // J Biol Chem 1983.- V.258.- № 3, — P 1086−1091.
- Poller L., Thomson J.M., Taberner D.A., Clarke D.K.The correction of coagulometer effects on international normalized ratios: a multicentre evaluation // Bi J Haematol. 1994 V.86.- № 1.-P.l 12−119.
- Ponce N.M., Pujol C.A., Damonte E.B., et al. Fucoidans from the brown seaweed Adenocystis utricularis: extraction methods, antiviral activity and structural studies // Carbohydrate Research, 2003, — V.338.- № 2, — P. 153−165.
- Porsche R., Brenner Z.R. Allergy to protamine sulfate // Heart Lung 1999.- V.28.- № 3,-P.418128.
- Pouplard C., Courvet C., Regina S., et al. Development of antibodies specific to polyanion-modified platelet factor 4 during treatment with fondaparinux // J Thromb Haemost 2005, — V.3.-№ 3, — P.2813−2818.
- Prandoni P., Biuchi O., Sabbion P., et al. Prolonged thromboprophylaxis with oral anticoagulants after total hip arthroplasty: a prospective controlled randomized study.// Arch Intern Med. 2002.- V.162.- № 17.- P. l966−1971.
- Preston F.W. The antihepann effect of Polybrene. (A polymer of N, N, N', N,-Tetramethylhexamethylenediamine and trimethylene bromide) // J Lab Clin Med 1952.- V.40.-№ 3.- P.927.
- Pugsley M.K., Kalra V., Froebel-Wilson S. Protamine is a low molecular weight polycationic amine that produces actions on cardiac muscle // Life Sci. 2002.- V.72.- P.293−305.
- Rabenstein D.L. Heparin and heparan sulfate: structure and function // Nat. Prod. Rep. 2002.- V.19.- № 3, — P.312−331.
- Racanelli A., Hoppensteadt D.A., Fareed J. In vitro protamine neutralization profiles of heparins differing in source and molecular weight // Semin Thromb Hemostasis. 1989.- V. l5.- № 4,-P.386−389.
- Racanelli A., Fareed J. Neutralization of the antithrombotic effects of heparin and Fraxiparin by protamine sulfate // Thrombosis Research 1992, — V.68.- № 3.- P.211−222.
- Redman A.R. Implications of cytochrome P450 2C9 polymorphism on warfarin metabolism and dosing // Pharmacotherapy 2001, — V.21.- № 2.-P.235−242.
- Refino C.J., Jeet S., DeGuzman L., et al. A human antibody that inhibits factor IX/IXa function potently inhibits arterial thrombosis without increasing bleeding // Arterioscler Thromb Vase Biol. 2002, — V.22.- № 3, — P.517−522.
- Rent R., Ertel N., Eisenstein R., Gewurz H. Complement activation by interaction of polyanions and polycations. I. Heparin-protamine induced consumption of complement // J. Immunol. 1975.-V.l 14,-№ 2, — P.120- 124.
- Rezaie A.R. Heparin chain-length dependence of factor Xa inhibition by antithrombin in plasma// Thrombosis Research 2007.- V. l 19, — № 4, — P.481−488.
- Rezaie A.R. Prothrombin protects factor Xa in the prothrombinase complex from inhibition by the heparin-antithrombin complex // Blood. 2001.- V.97.- № 5, — P.2308−2313.
- Ridker P.M., Goldhaber S.Z., Danielson E., et al. Long-term, low-intensity warfarin therapy for the prevention of recurrent venous thromboembolism // N Engl J Med 2003, — V.348.- № 2.-P. 1425−1434.
- Rijken D.C., Wijngaards G., Welbergen J. Immunological characterization of plasminogen activator activities in human tissue and body fluids // J Lab Clin Med 1981, — V.97.- № 3.-P477−563.
- Robinson H. С., Horner А. А., Но"о"к М&bdquo- et al proteoglycan form of heparin and its degradation to singlechain molecules // J. Biol. Chem. 1978, — V.253.- № 12.- P.6687−6693.
- Robson R. The use of bivalirudin in patients with renal impairment // J Invasive Cardiol. 2000.- V.12.- № 10.- P.33F-36 °F.
- Rosa A.T., Rotshild A.M., Rotshild Z. Fibrinolytic activity evoked in plasma of the normal and adrenalectomized rat by cellulose sulfate // Br J Pharmacol 1972, — V.45.- № 3, — P.470−475.
- Rosenberg R.D. Biological actions of heparin // Siminars in Hematology, 1977, — V.14.-№ 1.- P.427 — 440.
- Ross D.N. Theophylline-ethylenediamine in the measurement of blood circulation time // Br Heart J. 1951.- V.13.- № 5.- P.56−60.
- Rossmann P., Matousovic К., Horacek V. Protamineheparin aggregates, their fine structure, histochemistry and renal deposition. Virchows Archiv 1982, — V.40.- P.81−98.
- Salmivirta M., Lidholt K., Lindahl U. Heparan sulfatc: a piece of information // FASEB J. 1996.- V.10.- № 1, — P.1270−1279.
- Salzman E.W., Rosenberg R.D., Smith M.H., et al. Effect of Heparin and Heparin Fractions on Platelet Aggregation // J Clin Invest. 1980, — V. 65.- № 3. P.64−73.
- Salzman E.W., Rosenberg R.D., Smith M.H., et al. Effect of heparin and heparin fractions on platelet aggregation // J Clin Invest 1980.- V.65.- № 3.- P.64−73.
- Samama M.M., Gerotziafas G.T. Evaluation of the pharmacological properties and clinical results of the synthetic pentasaccharide (fondaparinux) // Thromb Res. 2003, — V.109.- P. 1−11
- Sandeep Chauhan, Bisoi Akshay Kumar, Beeraka Heramba Rao, et al. Efficacy of aprotinin, epsilon aminocaproic acid, or combination in cyanotic heart disease // Ann Thorac Surg2000, — V.70.- № 5, — P. 1308−1312
- Sanderson R. D. Heparan sulfate proteoglycans in invasion and metastasis // Semin. Cell Dev. Biol. 2001.- V. 12, — № 2, — P.89−98-
- Sanmartin M., Bonvini R. F., Verin V., et al. Bivalirudin in Acute Coronary Syndromes // N Engl J Med 2007.- V.356.-№ 2.- P. 1069−1071.
- Sasisekharan R., Shriver Z., Venkataraman G., Narayanasami U. Nat. Rev. Cancer 2002,-V.2.- № 3.- P.521−528.
- Sasisekharan R., Venkataraman G. Heparin and heparan sulfate: biosynthesis, structure and function// Curr. Opin. Chem.Biol. 2000, — V.4.- № 6.- P.626−631.
- Satomi O., Yoshitaka N., Sunao H., et al. Human antithrombin Ill-derived heparin-binding peptide, a novel heparin antagonis // Life Sciences 2003.- V.73.- № 3, — P.2793−2806.
- Schick B.P., Gradowski J.F., San Antonio J.D., Martinez J. Novel design of peptides to reverse the anticoagulant activities of heparin and other glycosaminoglycans // Thromb. Haemost.2001.-V.85.-№ 3.-P.482−487.
- Schjetlcin R., Sletnes K.E., Wishnff F. A quantitative, semi-automated and computer-assisted test for lupus anticoagulant // Thromb Res 1993, — V.69.- № 1.- P.239−250.
- Schulman S., Hellgren-Wangdahl M. Pregnancy, heparin and osteoporosis // Thromb Haemost 2002.- V.87.- № 3.- P. 180−181.
- Scully M.F., Ellis V., Shah N., Kakkar V. Effect of a heparan sulphate with high affinity for antithrombin III upon inactivation of thrombin and coagulation Factor Xa // Bioch J, 1989.-V.262.- № 2, — P.651−568.
- Serruys P.W., Herrman J.P., Simon R., et al. Acomparison of hirudin with heparin in the prevention of restenosis after coronary angioplasty. Helvetica Investigators // N Engl J Med. 1995.-V.333.- № 1.- P.757−763.
- Sharath M.D., Metzger W.J., Richerson H.B., et al., Protamineinduced fatal anaphylaxis: prevalence of antiprotamine immunoglobulin E antibody // J. Thorac. Cardiovasc. Surg. 1985.-V.90.- № 1.- P.86−90.
- Shenoy S., Harris R.B., Sobel M., Development of heparin antagonists with focused biological activity // Curr. Pharm. 1999, — V.5.- № 2, — P.965- 986.
- Shigemasa Y., Saito K., Sashiwa H., Saimoto H. Enzymatic degradation of chitins and partially deacetylated chitins // Int J Biol Macromol. 1994.-V.16, — №l.-P.43−49.
- Siragusa S., Cosmi В., Piovella F., et al. Low-molecularweight heparins and unfractionated heparin in the treatment of patients with acute venous thromboembolism: results of a meta-analysis //Am JMed 1996,-V. 100,-№ 4, — P.269−146.
- Skrzypczak-Jankun E., Carperos V.E. Ravichandran K.L., et al. Structure of the hirugen andhirulog 1 complexes of alpha-thrombin//J Mol Biol. 1991.- V221.- № 1.- P.1379−1393.
- Smith J.W., Kanuer D.J. A heparin binding site in antithrombin III // J Biol Chem 1987.-V.25.- № 2, — P. 11 964−12 034.
- Stuart R.K., Michel A. Monitoring heparin therapy with the activated partial thromboplastin time // Can Med Assotiation J, 1971, — V. l ()4.- № 6.- P.385−388.
- Suhara Y., Maruyama H.B., Koto Y., et al. A new antibiotic, fumaramidmycin. II. Isolation, structure and syntheses // J Antibiot (Tokyo). 1975, — V.28.- № 2.- P.648−703. 1
- Suraj G. Kamat, Alan Michelson, Stephen E. et al. Fibrinolysis Inhibits Shear Stress-Induced Platelet Aggregation // Circulation. 1995, — V.92.- № 2, — P.1399−1407.
- Taylor F.B. Jr. Role of tissue factor and factor Vila in the coagulant and inflammatory response to LD100 Escherichia coli in the baboon // Haemostasis. 1996.- V.26 .- J2.- P.83−91.
- Teien A.M., Lie M. Heparin assay in plasma a comparison of five clotting methods // Thromb Res. 1975, — V.7.- № 2, — P.777−788.
- Teien A.M., Lie M., Abilldgaard U. Assay of heparin in plasma using a chromogenic substrate for activated factor X // Thromb Res. 1976.- V.8.- № 3.- P.413−419.
- Teien A.N., Lie M. Evaluation of an amidolytic heparin assay method: increased sensitivity by adding purified antithrombin III // Thromb Res. 1977, — V.10.- № 5, — P.399−410.
- Thorsen S. The mechanism of plasminogen activation and the variability of the fibrin effector during tissue-type plasminogen activatorc- mediated fibrinolysis // Ann NY Acad Sci 1992, — V.301.- № 2, — P.52−63.
- Tinker J.H., Roberts S.L. Management of cardiopulmonary bypass. In // Kaplan JA, ed. Cardiac Anesthesia. 1987, — V.2.- № 2.- P.895−926.
- Tiu R. V., Kalmadi S. R., Lowe C., et al. Epsilon aminocaproic acid (EACA) is effective in controlling thrombocytopenic hemorrhage in patients with hematologic malignancies // Journal of Clinical Oncology, 2005.- V.23.- № 7, — P.6648−6652.
- Toida Т., Yoshida H., Toyoda H., et al. Structural Differences and the Presence of Unsubstituted Amino Groups in Heparan Sulphates from Different Tissues and Species // Biochem. J. 1997, — V.322.- № 1, — P.499−506.
- Tokura S., Nishi N., Nishimura S., Somorin O. Inhibition of the hydrolytic activity of thrombin by chitin heparinoids // Carbohydr Res. 1986. 1983.- V.15.- № 1, — P.-286−378.
- Tollefsen D.M., Peacock M. E, Monafo W.J. Molecular size of dermatan sulfate oligosaccharides required to bind and activate heparin cofactor II // J Biol Chem, 1986.- V.261.-№ 19, — P.8854−8912.
- Torjemanea L., Guermazib S. Ladeba S., et al Heparin-like anticoagulant associated with multiple myeloma and neutralized with protamine sulfate // Blood Coagulation and Fibrinolysis 2007, — V.18.- № 1.-P.279−281.
- Toschi V., Lettino M., Gallo R. et al. Biochemistry and biology of hirudin // Coron Artery Dis. 1996.- V.7.- № 7, — P.420−428.
- Toshiaki I., Akio K» Masaki F. et al. Factor Xa-Inhibitor (Dx-9065a) Modulates the Leukocyte-Endothelial Cell Interaction in Endotoxemic Rat // Shock. 2002 .- V.17.- N°2.- P.159−162.
- Trento F., Cattaneo F., Pescador R., et al. Antitrombin activity of an algae polysaccharide // Tromb. Res. 2001.- V.102.- № 5, — P.457−465.
- Turnbull J, Powell A., Guimond S. Heparan sulfate: decoding a dynamic multifunctional cell regulator // Trends Cell Biol. 2001.- V. l 1.- № 2, — P.75−82.
- Turnbull J. E. Integral glycan sequencing of hepaian sulfate and heparin saccharides. Methods Mol. Biol. 2001, — V. l71.- № 2.- P. 129−139.
- Turnbull J. E., Ilopwood J. J., Gallagher J. T. A strategy for rapid sequencing of heparan sulfate and heparin saccharides // Proc. Natl. Acad. Sci. U.S.A. 1999.- V.96.- № 4, — P.2698−2703.
- Turpie A.G., Bauer K.A., Eriksson B.I., et al. Postoperative fondaparinux versus postoperative enoxaparin for prevention of VTE after elective hipreplacement surgery: a randomised double-blind trial // Lancet. 2002, — V.359.- № 16, — P.1721−1726.
- Tyrrell D. J., Home A. P., Holme K.R., et al. Heparin in inflammation: potential therapeutic applications beyond anticoagulation // Adv. Pharmacol. 1999, — V.46.- № 3.- P.151−208.
- Van Walraven C., Hart R.G., Singer D.E., et al. Oral anticoagulants vs aspirin in nonvalvular atrial fibrillation: An individual patient meta-analysis // JAMA 2002, — V.288.- № 14,-P.2441−2448.
- Vermeer F., Vahanian A., Fels P.W., et al. Argatroban and alteplase in patients with acute myocardial infarction: the ARGAMI Study // J Thromb Thrombolysis. 2000, — V.10.- № 4, — P.233−240.
- Verrecchio A., Germann M.W., Schick B.P., et al. Design of peptides with high affinities for heparin and endothelial cell proteoglycans // J Biol Chem 2000, — V.275.- № 4, — P.7701−7708.
- Vikhoreva G., Bannikova G., Stolbushkina P., et al. Preparation and anticoagulant activity of a low-molecular-weight sulfated chitosan // Carbohydrate polymers 2005.- V.62.- №.4, — P.327−332.
- Violand B.N., Castellino F J. Mechanism of the urokinase-catalyzed activation of human plasminogen//J Biol Chem 1976.- V.251.- P.3906−3918.
- Vismara E., Pierini M., Guglieri S., et al. Structural Modification Induced in Heparin by a Fenton-Type Depolymerization Process Semin // Thiomb Hemost. 2007.- V.33.- № 3.- P.466−477.
- Volpi N. Characterization of heparins with different relative molecular masses (from 11,600 to 1600) by various analytical techniques // J Chromatogr. 1993, — V.622.- № 1, — P. 13−20.
- Vyas К.Л., Patel H.V., Vyas A.A.. Wu W. Glycosaminoglycans bind to homologous cardiotoxins with different specificity // Biochemistry. 1998.- V.37.- № 13, — P.4527−4534.
- Wagenvoord R., Dieri R.A., van Dedem G., et al, Linear diffusion of thrombin and factor Xa along the heparin molecule explains the effects of extended heparin chain lengths // Thrombosis Research 2008, — V.122.- № 2, — P.237−282.
- Wakefield T.W., Bouffard J.A., Spaulding S.A., et al. Sequestration of platelets in the pulmonary circulation as a consequence of protamine reversal of the anticoagulant effects of heparin // J Vase Surg 1987.- V.5.- № 2, — P. 187−280.
- Wakefield T.W., Andrews P.C., Wrobleski S.K., et al. Effective and less toxic reversal of low-molecular weight heparin anticoagulation by a designer variant of protamine // J Vase Surgery 1995.- V.21.- № 4, — P.839−49.
- Wakefield T.W., Andrews P.C., Wrobleski S.K., et al. A +18RGD. protamine variant for nontoxic and effective reversal of conventional heparin and low molecular weight heparin anticoagulation // J Surg Res 1996.- V.63.- № 7.- P.280−286.
- Walenga J., Jeske W., Hoppensteadt D., Fareed J. Factor Xa inhibitors: Today and beyong // Cur Opin invest Drugs 2003.- V.4.-№ 3.- P.272−281.
- Wall D., Douglas S., Ferro V., et al. Characterisation of the anticoagulant properties of a range of structurally diverse sulfated oligosaccharides // Thromb Res. 2001, — V.103.- № 4.- P.325−360.
- Wallis R.B. Hirudins: from leeches to man // Semin Thromb Hemost. 1996.- V.22.- № 6.-P.185−196.
- Wang W., Bo S., Li S., Qin W. Determination of the Mark-Houwink equation for chitosans with different degrees of deacetylation // Int J Biol Macromol 1991, — V. 13.- № 5, — P.281−286.
- Warda M., Mao W., Toida Т., Linhardt R. J. Turkey intestine as a commercial source of heparin? Comparative structural studies of intestinal avian and mammalian glycosaminoglycans // Сотр. Biochem. Physiol. 2003.-V, 134.-№ 11.-P. 189−197.
- Warkentin Т.Е., Levine M.N., Hirsh J., et al. Heparin-induced thrombocytopenia in patients treated with low molecular weight heparin or unfractionated heparin // N Engl J Med 1995, — V.332.-№ 2.- P.1330−1335.
- Weitz J.I. Low-molecular-weight heparins // New Engl J Med 1997, — V.337.- № 10, — P.688−698.
- Weitz J.I., Buller H.R. Direct thrombin inhibitors in acute coronary syndromes: present and future // Circulation. 2002, — V.105.- № 8, — P.1004−1011.
- Wessel H. P., Bartsch S. Conformational flexibility in highly sulfated beta-D-glucopyranoside derivatives // Carbohydr Res. 1997, — V.8.- № 274, — P. 1−9.
- Wessler S., Reimer S.M., Sheps M.C. Biologic assay of a thrombosis-inducing activity in human serum // J. Appl Physiol 1959.- V. 14, — № 1.- P.943−946.
- Whinna H.C., Blinder M.A., Szcwczyk M., et al. Role of lysine 173 in heparin binding to heparin cofactor II // J Biol Chem, 1991.- V.266.- № 13.- P.8129−8164.
- Whitelock J. M., Iozzo R. V. Heparan sulfate: a complex polymer charged with biological activity // Chem. Rev. 2005, — V. l05.- № 7.- P.2745−2764.
- Xin H., Thomas J. Girard, Pamela Baum, et al. Structural Requirements for TFPI-Mediated Inhibition of Neointimal Thickening After Balloon Injury in the Rat Arteriosclerosis // Thromb Vase Biol. 1999, — V.19.-№ 3.- P.2563−2567.
- Yamada S., Sugahara K. Structure of oligosaccharides isolated from heparan sulfate and heparin and substrate specificities of the degrading enzymes of bacterial origin // Trends Glycosci.Glycotechnol. 1998.- V.10.- № 6, — P.95−123.
- Yamagishi R., Niwa M., Sakuragawa N. Thrombin inhibitory activity of heparin cofactor II depends on the molecular weight and sulfate amount of dextran sulfate // Thromb Res. 1986.-V.44.- № 3.- P.347−401.
- Yates E. A., Guimond S. E., Turnbull J. E. Highly diverse heparan sulfate analogue libraries: providing access to expanded areas of sequence space for bioactivity screening // J. Med. Chem. 2004, — V.47.- № 1.- P.277−280.
- Yin E.T., Wessler S., Butler J.V. Plasma heparin: a unique, practical, submicrogram-sensitive assay // J Lab Clin Med. 1973, — V.81.- № 2.- P.298−310.
- Yokoyama Т., Hosaka Y., Takagi S. The place of chemical leeching with heparin in digital replantation: subcutaneous calcium hepaiin for patients not treatable with systemic heparin // Plast Reconstr Surg. 2007, — V. 119, — № 4.- P. 1284−1377.
- Young E., Cosmi В., Weitz J., Hirsh J. Comparison of the non-specific binding of unfractionated heparin and low molecular weight heparin (enoxaparin) to plasma proteins // Thromb Haemost 1993 V.70.- № 1, — P.625- 655.
- Yu G., Gunay N.S., Linhardt R.J., Toida Y., et al. Preparation and anticoagulant activity of the phosphosulfomannan PI-88 // Eur J Med Chem. 2002, — V37.- № 10.- P.783−874.
- Zaikov G.E. Degradation and Stabilization of Polymers // N.Y.:Nova Sci. Publ., 1999.-P.296.
- Zanon C» Bortolini M., Chiappino I. Low-molecular-weight heparin and calcium heparin in thrombosis prophylaxis in patients with percutaneous arterial and venous ports for colorectal liver metastases // Tumor 2005, — V.91.- № 6, — P.477−557.
- Zhang D., Raghavan N., Chen S.Y., et al. Reductive isoxazole ring-opening of the anticoagulant razaxaban is the major metabolic clearance pathway in rats and dogs // Drug Metab Dispos. 2008, — V.36.- № 2.- P.303−318.