Interaction of Factor XIa and Antithrombin in the Presence
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چکیده
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 iO8 mol/L. 5.76 x iO mol/L. and either 5.88 x iO 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 -i.O mm’ and -0.025 min . respectively.
منابع مشابه
Interaction of factor XIa and antithrombin in the presence and absence of heparin.
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 fac...
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The effect of various well-characterized heparin preparations on the inactivation of human Factor XIa by human antithrombin III was studied. The heparin preparations used were unfractionated heparin and four heparin fractions obtained after anion-exchange chromatography. Inactivation of Factor XIa was monitored with S2366 as chromogenic substrate and followed pseudo-first-order reaction kinetic...
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Human factor IX circulates as a single-chain glycoprotein. Upon activation in vitro, it is cleaved into disulfide-linked light and heavy chains and an activation peptide. After reduction of activated 125I-factor IX, the heavy and light chains are readily identified by gel electrophoresis. A direct, immunoradiometric assay for factor IXa was developed to assess activation of factor IX for protea...
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The control of coagulation enzymes by antithrombin is vital for maintenance of normal hemostasis. Antithrombin requires the co-factor, heparin, to efficiently inhibit target proteinases. A specific pentasaccharide sequence (H5) in high affinity heparin induces a conformational change in antithrombin that is particularly important for factor Xa (fXa) inhibition. Thus, synthetic H5 accelerates th...
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Heparin fractions of different molecular weight and with high affinity for antithrombin were studied with respect to their ability to potentiate the inhibition of activated clotting factors by antithrombin. Inhibition of thrombin, Factor IXa and Factor XIa showed similarities in the dependence on the molecular weight of heparin and was found to decrease with decreasing molecular weight. Inactiv...
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تاریخ انتشار 2005