作者: Robert F. Highsmith , Robert D. Rosenberg
DOI: 10.1016/S0021-9258(19)42424-1
关键词: Sodium dodecyl sulfate 、 Cofactor 、 Gel electrophoresis 、 Enzyme 、 Molecular biology 、 Antithrombin 、 Biochemistry 、 Plasmin 、 Incubation 、 Chemistry 、 Heparin
摘要: Abstract The interaction of purified human antithrombin-heparin cofactor and plasmin was studied in the presence absence heparin. Antithrombin is a progressive, timedependent inhibitor proteolytic esterolytic activities plasmin. Incubation with antithrombin for 15 to 30 min results 90 100% inhibition both enzyme. heparin dramatically accelerates rate plasmin, nearly complete within s incubation. Sodium dodecyl sulfate gel electrophoresis reduced nonreduced proteins indicates that functions as potent antiplasmin by forming an undissociable complex which stable denaturing or reducing agents (or both). This represents 1:1 stoichiometric combination enzyme inhibitor. Heparin increases formation this without affecting its dissociability stoichiometry.