Proteolytic interactions of factor IXa with human factor VIII and factor VIIIa

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Proteolytic interactions of factor IXa with human factor VIII and factor VIIIa.

Factor IXa was shown to inactivate both factor VIII and factor VIIIa in a phospholipid-dependent reaction that could be blocked by an antifactor IX antibody. Factor IXa-catalyzed inactivation correlated with proteolytic cleavages within the A1 subunit of factor VIIIa and within the heavy chain (contiguous A1-A2-B domains) of factor VIII. Furthermore, a relatively slow conversion of factor VIII ...

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Proteolytic Interactions of Factor IXa With Human Factor VI11 and Factor VIIIa

Factor IXa was shown to inactivate both factor Vlll and factor Vllla in a phospholipid-dependent reaction that could be blocked by an antifactor IX antibody. Factor IXa-catalyzed inactivation correlated with proteolytic cleavages within the A1 subunit of factor Vllla and within the heavy chain (contiguous AI-A2-6 domains) of factor VIII. Furthermore, a relatively slow conversion of factor Vlll ...

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Activation of factor VIII by factor IXa.

Thrombin causes an increase in factor VIII coagulant (VIII:C) activity, which is followed by a decay of VIII:C activity to below baseline levels. It has been suggested that a similar interaction of trace amounts of thrombin and factor VIII is a necessary prerequisite before factor VIII can participate in the coagulation cascade. In the current study, factor IXa, a serine protease with structura...

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Kinetics of Factor X activation by the membrane-bound complex of Factor IXa and Factor VIIIa.

Intrinsic tenase consists of activated Factors IX (IXa) and VIII (VIIIa) assembled on a negatively charged phospholipid surface. In vivo, this surface is mainly provided by activated platelets. In vitro, phosphatidylcholine/phosphatidylserine vesicles are often used to mimic natural pro-coagulant membranes. In the present study, we developed a quantitative mathematical model of Factor X activat...

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ژورنال

عنوان ژورنال: Blood

سال: 1992

ISSN: 0006-4971,1528-0020

DOI: 10.1182/blood.v80.12.3120.bloodjournal80123120