Title : Studies on human antihemophilic factor. Evidence for a covalently linked subunit structure.

Pub. Date : 1976 Apr

PMID : 1084890






1 Functional Relationships(s)
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1 When purified antihemophilic factor (Factor VIII) was rechromatographed on 4% agarose in 0.15 M NaCl or 1.0 M NaCl, a single protein peak, containing both procoagulant activity and von Willebrand factor activity, as defined by ristocetin-induced platelet aggregation, was eluted in the void volume. Sepharose coagulation factor VIII Homo sapiens