= D. L. Higgins
{c}
<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>.<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]{ref}
At $37\,{}^{\circ}\mathrm{C}$ 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.<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]{ref}
Back to article page
