Measurement of the kinetic parameters mediating protease–serpin inhibition
作者： N Schechter
DOI: 10.1016/S1046-2023(03)00207-X
关键词:
摘要: Serine protease inhibition by proteins of the serpin family is a unique and complex process involving physical, chemical, conformational changes. After encounter with reactive site inhibitor, conformationally trapped as covalent resembling acyl-protease intermediate catalysis. The stability trap not permanent may vary for different proteases. In addition, trapping mechanism 100% efficient fraction be consumed like substrate before inactivation complete. Characterization protease-serpin therefore requires measurement three parameters: apparent second order rate constant (k(inh)), stoichiometry (SI), breakdown (k(brkdn)). basic kinetic methods to establish these parameters are described.
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sci-hub.se 参考文章(38)
S E Szedlacsek, V Ostafe, R G Duggleby, M Serban, M O Vlad, Progress-curve equations for reversible enzyme-catalysed reactions inhibited by tight-binding inhibitors. Biochemical Journal. ,vol. 265, pp. 647- 653 ,(1990) , 10.1042/BJ2650647
Jacqueline A. Reynolds, Charles Tanford, The Gross Conformation of Protein-Sodium Dodecyl Sulfate Complexes Journal of Biological Chemistry. ,vol. 245, pp. 5161- 5165 ,(1970) , 10.1016/S0021-9258(18)62831-5
H Rubin, Z M Wang, E B Nickbarg, S McLarney, N Naidoo, O L Schoenberger, J L Johnson, B S Cooperman, Cloning, expression, purification, and biological activity of recombinant native and variant human alpha 1-antichymotrypsins. Journal of Biological Chemistry. ,vol. 265, pp. 1199- 1207 ,(1990) , 10.1016/S0021-9258(19)40178-6
N M Schechter, J L Sprows, O L Schoenberger, G S Lazarus, B S Cooperman, H Rubin, Reaction of human skin chymotrypsin-like proteinase chymase with plasma proteinase inhibitors. Journal of Biological Chemistry. ,vol. 264, pp. 21308- 21315 ,(1989) , 10.1016/S0021-9258(19)30080-8
N.M. Schechter, L.M. Jordan, A.M. James, B.S. Cooperman, Z.M. Wang, H Rubin, Reaction of human chymase with reactive site variants of alpha 1-antichymotrypsin. Modulation of inhibitor versus substrate properties. Journal of Biological Chemistry. ,vol. 268, pp. 23626- 23633 ,(1993) , 10.1016/S0021-9258(19)49508-2
B.S. Cooperman, E Stavridi, E Nickbarg, E Rescorla, N.M. Schechter, H Rubin, Antichymotrypsin interaction with chymotrypsin. Partitioning of the complex. Journal of Biological Chemistry. ,vol. 268, pp. 23616- 23625 ,(1993) , 10.1016/S0021-9258(19)49507-0
S T Olson, Heparin and ionic strength-dependent conversion of antithrombin III from an inhibitor to a substrate of alpha-thrombin. Journal of Biological Chemistry. ,vol. 260, pp. 10153- 10160 ,(1985) , 10.1016/S0021-9258(17)39226-8
P A Patston, N Roodi, J A Schifferli, R Bischoff, M Courtney, M Schapira, Reactivity of alpha 1-antitrypsin mutants against proteolytic enzymes of the kallikrein-kinin, complement, and fibrinolytic systems. Journal of Biological Chemistry. ,vol. 265, pp. 10786- 10791 ,(1990) , 10.1016/S0021-9258(18)87016-8
L C Petersen, I Clemmensen, Kinetics of plasmin inhibition in the presence of a synthetic tripeptide substrate. The reaction with pancreatic trypsin inhibitor and two forms of α 2-plasmin inhibitor Biochemical Journal. ,vol. 199, pp. 121- 127 ,(1981) , 10.1042/BJ1990121
Kevin M. O'Malley, Shrikumar A. Nair, Harvey Rubin, Barry S. Cooperman, The Kinetic Mechanism of Serpin-Proteinase Complex Formation Journal of Biological Chemistry. ,vol. 272, pp. 5354- 5359 ,(1997) , 10.1074/JBC.272.8.5354