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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
1996-7-1
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pubmed:abstractText |
Hamster cheek pouch vascular tissues contain an angiotensin II-forming enzyme which is inhibited by chymostatin but not by any angiotensin-converting enzyme inhibitors. The enzyme was purified to apparent homogeneity by gel filtration and heparin-Sepharose affinity chromatography. The molecular mass estimated by sodium dodecyl sulphate polyacrylamide gel electrophoresis was 28 kDa and the optimum pH was between 7.5 and 9.0. The angiotensin II-forming activity was inhibited by chymostatin, soybean trypsin inhibitor and phenylmethylsulfonyl fluoride, but not by aprotinin. The N-terminal sequence showed high homology with chymases from various species. Thus, the angiotensin II-generating enzyme obtained from hamster cheek pouch vessels is a chymase.
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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:issn |
0024-3205
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
58
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
591-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8632712-Amino Acid Sequence,
pubmed-meshheading:8632712-Angiotensin II,
pubmed-meshheading:8632712-Animals,
pubmed-meshheading:8632712-Cheek,
pubmed-meshheading:8632712-Chromatography, Affinity,
pubmed-meshheading:8632712-Chromatography, Gel,
pubmed-meshheading:8632712-Chromatography, High Pressure Liquid,
pubmed-meshheading:8632712-Chymases,
pubmed-meshheading:8632712-Cricetinae,
pubmed-meshheading:8632712-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:8632712-Humans,
pubmed-meshheading:8632712-Male,
pubmed-meshheading:8632712-Molecular Sequence Data,
pubmed-meshheading:8632712-Sequence Homology, Amino Acid,
pubmed-meshheading:8632712-Serine Endopeptidases
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pubmed:year |
1996
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pubmed:articleTitle |
Purification and characterization of angiotensin II-generating chymase from hamster cheek pouch.
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pubmed:affiliation |
Department of Pharmacology, Osaka Medical College, Japan.
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pubmed:publicationType |
Journal Article
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