1. The supernatant obtained by centrifugation of a rat liver homogenate at 100000g for 1h contained a heat-labile macromolecular inhibitor of the thrombin–fibrinogen reaction. 2. The inhibitor was purified to electrophoretic homogeneity by repeated preparative polyacrylamide disc electrophoresis. Inhibition was observed with purified inhibitor equivalent to about 1μg of protein/ml. 3. The inhibitor had a pI of 3.50–3.75, a molecular weight (from sodium dodecyl sulphate–polyacrylamide-gel electrophoresis) of 72000±3000 and was inactivated by p-hydroxymercuribenzoate or 5,5′-dithiobis-(2-nitrobenzoic acid). 4. Kinetic studies revealed a non-competitive inhibition, with the inhibitor probably acting on the thrombin–fibrinogen complex.
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Research Article| August 01 1972
Inhibition of the thrombin–fibrinogen reaction by a macromolecular factor from rat liver
Ragnar Flengsrud ;
Bjarne Østerud ;
Biochem J (1972) 129 (1): 83–89.
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Ragnar Flengsrud, Bjarne Østerud, Hans Prydz; Inhibition of the thrombin–fibrinogen reaction by a macromolecular factor from rat liver. Biochem J 1 August 1972; 129 (1): 83–89. doi: https://doi.org/10.1042/bj1290083
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