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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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Published in: | FEBS letters 1999-08, Vol.456 (2), p.290-294 |
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Main Authors: | , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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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. |
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ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/S0014-5793(99)00959-X |