| Literature DB >> 10456326 |
A Hunfeld1, M Etscheid, H König, R Seitz, J Dodt.
Abstract
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. NH2-terminal sequence analysis revealed identity to the deduced amino acid sequence of HGFA-like mRNA. The activity of PHBSP is strongly dependent on Ca2+ ions and is efficiently inhibited by alpha2-antiplasmin and aprotinin. Possible functions of PHBSP in the hemostatic system are discussed.Entities:
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Year: 1999 PMID: 10456326 DOI: 10.1016/s0014-5793(99)00959-x
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124