Kinetic properties of the primary inhibitor of plasmin from human plasma
- 1 May 1977
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 163 (2) , 389-391
- https://doi.org/10.1042/bj1630389
Abstract
The interaction of human plasmin with the newly discovered .alpha.2-plasmin inhibitor was investigated. Rate measurements indicated that the reaction involves the rapid formation of a 1st enzyme-inhibitor complex, followed by the slow irreversible transition to another complex. L-Lysine influences the 1st step, but not the 2nd.This publication has 10 references indexed in Scilit:
- Kinetic studies of the urokinase catalysed conversion of NH2-terminal lysine plasminogen to plasminBiochimica et Biophysica Acta (BBA) - Enzymology, 1977
- The primary inhibitor of plasmin in human plasmaBiochemical Journal, 1976
- Isolation and characterization of alpha2-plasmin inhibitor from human plasma. A novel proteinase inhibitor which inhibits activator-induced clot lysis.Journal of Biological Chemistry, 1976
- Identification and Some Properties of a New Fast‐Reacting Plasmin Inhibitor in Human PlasmaEuropean Journal of Biochemistry, 1976
- pH effects in plasmin-catalysed hydrolysis of
benzoyl- compoundsl -arginineBiochimica et Biophysica Acta (BBA) - Enzymology, 1975 - Immunochemical distinction between antiplasmin and alpha1-antitrypsinThrombosis Research, 1975
- Different molecular forms of plasminogen and plasmin produced by urokinase in human plasma and their relation to protease inhibitors and lysis of fibrinogen and fibrinBiochemical Journal, 1974
- Comparison of the esterase activities of trypsin, plasmin, and thrombin on guanidinobenzoate esters. Titration of the enzymesBiochemistry, 1969
- Elementary Steps in Enzyme Reactions (as Studied by Relaxation Spectrometry)Published by Wiley ,1963