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• W2032536738 startingPage "159" @default.
• W2032536738 abstract "Serine protease inhibition by proteins of the serpin family is a unique and complex process involving physical, chemical, and conformational changes. After encounter with the reactive site of inhibitor, the protease is conformationally trapped as a covalent complex resembling the acyl-protease intermediate of catalysis. The stability of the trap is not permanent and may vary for different proteases. In addition, the trapping mechanism is not 100% efficient and a fraction of the serpin may be consumed like a substrate before inactivation is complete. Characterization of protease-serpin inhibition therefore requires the measurement of three parameters: the apparent second order rate constant of inhibition (k(inh)), the stoichiometry of inhibition (SI), and the rate of complex breakdown (k(brkdn)). The basic kinetic methods to establish these parameters are described." @default.
• W2032536738 created "2016-06-24" @default.
• W2032536738 creator A5000644404 @default.
• W2032536738 creator A5016767897 @default.
• W2032536738 date "2004-02-01" @default.
• W2032536738 modified "2023-09-23" @default.
• W2032536738 title "Measurement of the kinetic parameters mediating protease–serpin inhibition" @default.
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• W2032536738 doi "https://doi.org/10.1016/s1046-2023(03)00207-x" @default.
• W2032536738 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/14698628" @default.
• W2032536738 hasPublicationYear "2004" @default.
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