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Реферати, твори, дипломи, практика » Курсовые обзорные » Експериментальне дослідження активації системи згортання ферментами фібринолізу

Реферат Експериментальне дослідження активації системи згортання ферментами фібринолізу





Plow EF. The cell-binding domains of plasminogen and their function in plasma. J Biol Chem. 1988; 263:11928-11934. p align="justify">. Henschen A. On the structure of functional sites in fibrinogen. Thromb Res. 1983; Suppl V: 27-39. p align="justify">. Darras V, Thienpont M, Stump DC, Collen D. Measurement of urokinase-type plasminogen activator (u-PA) with an enzyme-linked immunosorbent assay (ELISA) based on three murine monoclonal antibodies. Thromb Haemost. 1986; 56:411-414. p align="justify">. Ellis V, Scully MF, Kakkar VV. Plasminogen activation by single-chain urokinase in functional isolation. A kinetic study. J Biol Chem. 1987; 262:14998-15003. p align="justify">. Lijnen HR, Van Hoef B, De Cock F, Collen D. The mechanism of plasminogen activation and fibrin dissolution by single chain urokinase-type plasminogen activator in a plasma milieu in vitro. Blood. 1989; 73:1864-1872. p align="justify">. Andreasen PA, Nielsen LS, Kristensen P, Grondahl-Hansen J, Skriver L, Dano K. Plasminogen activator inhibitor from human fibrosarcoma cell binds urokinase-type plasminogen activator, but not its proenzyme. J Biol Chem. 1 986; 261:7644-7651. p align="justify">. Gurewich V, Pannell R, Louie S, Kelley P, Suddith RL, Greenlee R. Effective and fibrin-specific clot lysis by a zymogen precursor form of urokinase (pro-urokinase). A study in vitro and in two animal species. J Clin Invest. 1984; 73:1731-1739. p align="justify">. Robbie LA, Bennett B, Croll AM, Brown PA, Booth NA. Proteins of the fibrinolytic system in human thrombi. Thromb Haemost. 1996; 75:127-133. p align="justify">. van Zonneveld AJ, Veerman H, Pannekoek H. On the interaction of the finger and the kringle-2 domain of tissue-type plasminogen activator with fibrin. Inhibition of kringle-2 binding to fibrin by epsilon-amino caproic acid. J Biol Chem. 1986; 261:14214-14218. p align="justify">. Madison EL, Goldsmith EJ, Gerard RD, Gething MJ, Sambrook JF, Bassel-Duby RS. Amino acid residues that affect interaction of tissue-type plasminogen activator with plasminogen activator inhibitor 1. Proc Natl Acad Sci. 1990; 87:3530-3533. p align="justify">. Ranby M. Studies on the kinetics of plasminogen activation by tissue plasminogen activator. Biochim Biophys Acta. 1982; 704:461-469. p align="justify">. Tate KM, Higgins DL, Holmes WE, Winkler ME, Heyneker HL, Vehar GA. Functional role of proteolytic cleavage at arginine-275 of human tissue plasminogen activator as assessed by site-directed mutagenesis. Biochemistry. 1987; 26:338-343

. Wiman B, Collen D. On the kinetics of the reaction between human antiplasmin and a low-molecular-weight form of plasmin. Eur J Biochem. 1 978; 87:143-146. p align="justify">. Kolev K, Lerant I, Tenekejiev K, Machovich R. Regulation of fibrinolytic activity of neutrophil leukocyte elastase, plasmin and miniplasmin by plasma protease inhibitors. J Biol Chem. 1994; 269:17030-17034. p align="justify">...


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