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- W2343190012 endingPage "1492" @default.
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- W2343190012 abstract "Abstract We have studied the interaction between purified human factor XIa and antithrombin in the presence and absence of well-characterized preparations of heparin. The concentrations of hemostatic enzyme, protease inhibitor, and mucopolysaccharide were 5.76 X 10(-8) mol/L, 5.76 X 10(6) mol/L, and either 5.88 X 10(6) mol/L or 0, respectively. Kinetic investigation of this process using a tritiated factor IX substrate demonstrated that the pseudo first-order rate constants of this reaction in the presence and absence of heparin are approximately 1.0 min-1 and approximately 0.025 min-1, respectively. Thus, the rate of hemostatic enzyme-protease inhibitor complex formation is accelerated by about 40-fold in the presence of saturating levels of the mucopolysaccharide. These results were confirmed in a qualitative manner by directly monitoring the generation of factor XIa-antithrombin interaction product with sodium dodecyl sulfatepolyacrylamide gel electrophoresis (SDS-PAGE) and Western blot analysis using an antibody population specific for the protease inhibitor." @default.
- W2343190012 created "2016-06-24" @default.
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- W2343190012 date "1986-05-01" @default.
- W2343190012 modified "2023-09-28" @default.
- W2343190012 title "Interaction of factor XIa and antithrombin in the presence and absence of heparin" @default.
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- W2343190012 doi "https://doi.org/10.1182/blood.v67.5.1488.1488" @default.
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