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Detection of a novel plasma serine protease during purification of vitamin K-dependent coagulation factors

A novel serine protease (PHBSP) was purified from human plasma by two chromatographic steps with a final yield of 1.6 mg/l plasma. The protease consists of two disulfide-bridged chains of about 50 and 30 kDa with the light chain containing the active site of the enzyme. NH 2-terminal sequence analys...

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Bibliographic Details
Published in:FEBS letters 1999-08, Vol.456 (2), p.290-294
Main Authors: Hunfeld, A, Etscheid, M, König, H, Seitz, R, Dodt, J
Format: Article
Language:English
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Summary:A novel serine protease (PHBSP) was purified from human plasma by two chromatographic steps with a final yield of 1.6 mg/l plasma. The protease consists of two disulfide-bridged chains of about 50 and 30 kDa with the light chain containing the active site of the enzyme. NH 2-terminal sequence analysis revealed identity to the deduced amino acid sequence of HGFA-like mRNA. The activity of PHBSP is strongly dependent on Ca 2+ ions and is efficiently inhibited by α 2-antiplasmin and aprotinin. Possible functions of PHBSP in the hemostatic system are discussed.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(99)00959-X