Detection of a novel plasma serine protease during purification of vitamin K-dependent coagulation factors. |
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| Authors: | A Hunfeld M Etscheid H K?nig R Seitz J Dodt |
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| Institution: | Paul-Ehrlich-Institut, Langen, Germany. hunan@pei.de |
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| 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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