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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1999-8-30
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pubmed:abstractText |
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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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
456
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
290-4
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10456326-Amino Acid Sequence,
pubmed-meshheading:10456326-Blood Coagulation Factors,
pubmed-meshheading:10456326-Catalytic Domain,
pubmed-meshheading:10456326-Cations, Divalent,
pubmed-meshheading:10456326-Chromatography, Ion Exchange,
pubmed-meshheading:10456326-Hemostasis,
pubmed-meshheading:10456326-Hepatocyte Growth Factor,
pubmed-meshheading:10456326-Humans,
pubmed-meshheading:10456326-Molecular Weight,
pubmed-meshheading:10456326-Protein Conformation,
pubmed-meshheading:10456326-Sequence Homology, Amino Acid,
pubmed-meshheading:10456326-Serine Endopeptidases,
pubmed-meshheading:10456326-Serine Proteinase Inhibitors,
pubmed-meshheading:10456326-Substrate Specificity,
pubmed-meshheading:10456326-Vitamin K
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pubmed:year |
1999
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pubmed:articleTitle |
Detection of a novel plasma serine protease during purification of vitamin K-dependent coagulation factors.
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pubmed:affiliation |
Paul-Ehrlich-Institut, Langen, Germany. hunan@pei.de
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pubmed:publicationType |
Journal Article,
Comparative Study,
In Vitro
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