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Article

Peptide bond cleavages and loss of functional activity during inactivation of factor Va and factor VaR506Q by activated protein C.

The Journal of biological chemistry - 8 Sept 1995

Nicolaes G A, Tans G, Thomassen M C, Hemker H C, Pabinger I, Varadi K, Schwarz H P, Rosing J

Abstract excerpt

Factor V was purified from the plasma of an activated protein C (APC)-resistant patient who is homozygous for the mutation Arg506-->Gln (factor VR506Q). Factor VR506Q was converted by thrombin into factor Va which was further purified yielding a factor Va preparation that had the same cofactor activity in prothrombin activation as normal factor Va. Inactivation of low concentrations of normal factor Va (< 5 nM)...

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Identifiers

PMID: 7673148
DOI: 10.1074/jbc.270.36.21158

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APC

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Peptide bond cleavages and loss of functional activity during inactivation of factor Va and factor VaR506Q by activated protein C.PMID 7673148Read ↗

Factor Va is inactivated by activated protein C in the absence of cleavage sites at Arg-306, Arg-506, and Arg-679.Semantic proximity Read ↗

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Coagulation factor V: an old star shines again.Semantic proximity Read ↗

Detailed mechanisms of the inactivation of factor VIIIa by activated protein C in the presence of its cofactors, protein S and factor V.Semantic proximity Read ↗

The R306G and R506Q mutations in coagulation Factor V reveals additional cleavage sites for Activated Protein C in the R313-R321 region and at R505.Semantic proximity Read ↗

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Cleavage requirements for activation of factor V by factor Xa.Semantic proximity Read ↗

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