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. 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.
Hunfeld
A
A
Paul-Ehrlich-Institut, Langen, Germany. hunan@pei.de
Etscheid
M
M
König
H
H
Seitz
R
R
Dodt
J
J
D000595:Amino Acid Sequence; D001779:Blood Coagulation Factors / Q000302:isolation & purification*; D020134:Catalytic Domain; D002413:Cations, Divalent / Q000494:pharmacology; D002852:Chromatography, Ion Exchange; D006487:Hemostasis / Q000502:physiology; D017228:Hepatocyte Growth Factor / Q000378:metabolism; D006801:Humans; D066298:In Vitro Techniques; D008970:Molecular Weight; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000097:blood* / Q000235:genetics / Q000302:isolation & purification; D015842:Serine Proteinase Inhibitors / Q000494:pharmacology; D013379:Substrate Specificity; D014812:Vitamin K / Q000097:blood*
D001779:Blood Coagulation Factors; D002413:Cations, Divalent; D015842:Serine Proteinase Inhibitors; D014812:Vitamin K; D017228:Hepatocyte Growth Factor; C081092:HGF activator; D012697:Serine Endopeptidases