D. L. Higgins investigated the enzyme kinetics of thrombin, the enzyme that converts soluble fibrinogen into clot-forming fibrin. A 1983 study measured the release of Fibrinopeptide A and Fibrinopeptide B from human fibrinogen, separating the cutting of peptide bonds from the subsequent polymerization of fibrin.[ref]
Steady state kinetic parameters for the thrombin-catalyzed conversion of human fibrinogen to fibrin by D. L. Higgins and others. Journal of Biological Chemistry 258, pp. 9276–9282; abstract and kinetic measurements
At and pH 7.4, at least 97% of Fibrinopeptide B release followed Fibrinopeptide A release under the tested conditions. Inhibiting fibrin polymerization reduced Fibrinopeptide B release without reducing Fibrinopeptide A release. This intervention helped distinguish a sequence of coupled events: the first cleavage permits assembly, and assembly changes the later cleavage reaction. Simply measuring the final amount of fibrin would conceal that ordering.[ref]
Steady state kinetic parameters for the thrombin-catalyzed conversion of human fibrinogen to fibrin by D. L. Higgins and others. Abstract; sequential release and effects of polymerization inhibitors
Articles by others on the same topic
There are currently no matching articles.