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Article

Identification and partial characterization of factor Va heavy chain kinase from human platelets.

The Journal of biological chemistry - 3 Apr 1998

Kalafatis M

Abstract excerpt

Factor Va, the essential cofactor for prothrombinase, is phosphorylated on the acidic COOH terminus of the heavy chain of the cofactor, at Ser692, by a platelet membrane-associated casein kinase II (CKII). Consistent with this observation, phosphorylation of the factor Va heavy chain by the platelet kinase was inhibited by heparin. The membrane-associated platelet CKII kinase was partially purified using...

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PMID: 9525959
DOI: 10.1074/jbc.273.14.8459

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Identification and partial characterization of factor Va heavy chain kinase from human platelets.PMID 9525959Read ↗

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Role of Hirudin-like factor Va heavy chain sequences in prothrombinase function.Semantic proximity Read ↗

Proexosite-1 on prothrombin is a factor Va-dependent recognition site for the prothrombinase complex.Semantic proximity Read ↗

The interaction of prothrombin with phospholipid membranes is independent of either kringle domain.Semantic proximity Read ↗

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Asp-70-->Lys mutant of factor X lacks high affinity Ca2+ binding site yet retains function.Semantic proximity Read ↗

Amino acids Glu323, Tyr324, Glu330, and Val331 of factor Va heavy chain are essential for expression of cofactor activity.Semantic proximity Read ↗

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