Properties of human asialo-factor VIII. A ristocetin-independent platelet-aggregating agent.
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چکیده
منابع مشابه
Properties of human asialo-factor VIII. A ristocetin-independent platelet-aggregating agent.
Human Factor VIII desialylated by treatment with Vibrio cholerae neuraminidase (ASVIII) aggregated human platelets in the absence of ristocetin in platelet-rich plasma and, to a lesser extent, in washed platelet suspensions. Aggregation is accompanied by thromboxane formation and is completely inhibited by EDTA. Aspirin blocks the second phase of aggregation and abolishes thromboxane production...
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A monoclonal antibody to human antihemophilic factor (AHF. factor VIII) was derived from BALB/c mouse spleen cells fused with P3x63Ag8 mouse plasmacytoma cells. This antibody. harvested from culture medium or ascites fluid. reacted with purified AHF and with plasmas from normal subjects or classic hemophiliacs, as measured by enzymelinked immuonsorbant assay (ELISA). but not with plasmas from p...
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Studies of the functional properties and intravascular survival of normal and desialylated human Factor VIIIlvon Willebrand factor protein have been performed. The purified normal protein, possessing both procoagulant activity and ristecetin-induced platelet-aggregating activity, contains 154 = 15 nmol of sialic acid/mg of protein and 28 f 3 mol of Sk&k acid/m01 of 200,000 molecular weight subu...
متن کاملRelationship of sialic acid to function and in vivo survival of human factor VIII/von Willebrand factor protein.
Studies of the functional properties and intravascular survival of normal and desialylated human Factor VIIIlvon Willebrand factor protein have been performed. The purified normal protein, possessing both procoagulant activity and ristecetin-induced platelet-aggregating activity, contains 154 = 15 nmol of sialic acid/mg of protein and 28 f 3 mol of Sk&k acid/m01 of 200,000 molecular weight subu...
متن کاملAsialo-von Willebrand factor inhibits platelet adherence to human arterial subendothelium: discrepancy between ristocetin cofactor activity and primary hemostatic function.
Platelet adherence at high wall shear rates requires plasma von Willebrand factor (vWF). Clinically, the ristocetin cofactor (RCof) activity is the only widely available assay for vWF function. When purified vWF is treated with neuraminidase to yield asialo-vWF (AS-vWF), its RCof activity is increased by 20% to 40%. AS-vWF binds to normal human platelets independently of ristocetin and induces ...
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ژورنال
عنوان ژورنال: Journal of Clinical Investigation
سال: 1981
ISSN: 0021-9738
DOI: 10.1172/jci110259