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Comparative Study
. 1999 Aug 6;456(2):290-4.
doi: 10.1016/s0014-5793(99)00959-x.

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

A Hunfeld  1 , M Etscheid, H König, R Seitz, J Dodt
Affiliations
Free article
Comparative Study

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

A Hunfeld et al. FEBS Lett. .
Free article

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.

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