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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1976-11-21
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pubmed:abstractText |
Human high molecular weight kininogen was isolated by a rapid procedure, using anion exchange chromatography on QAE-Sephadex, ammonium sulfate precipitation and cation exchange chromatography on CM-Sephadex. The poor recovery and relatively low specific activity observed in earlier experiments was found to be due to a contaminant, presumably enzymatic, capable of releasing kinin from the kininogen. The "spontaneous" kinin release was blocked by soy bean trypsin inhibitor and by C1-inactivator. The isolated kininogen was stable at different temperatures, did not contain free kinin and was a good substrate for plasma kallikrein and plasmin.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0065-4299
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
565-8
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading | |
pubmed:year |
1976
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pubmed:articleTitle |
Rapid purification of human high molecular weight kininogen.
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pubmed:publicationType |
Journal Article
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