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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
1992-3-3
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pubmed:abstractText |
A calpain (Ca(2+)-activated neutral protease) activator was purified from human platelets by ammonium sulfate fractionation, gel-filtration, ion-exchange chromatography, followed by heat-treatment. The purified calpain activator with a Mr of 47.5 kDa was a heat-stable protein as demonstrated in other cells. The calpain activator did not change the Ca2+ sensitivity of calpain but activated calpain activity about 2-fold. This calpain activator may play an important role in the activation of the protease system leading to the Ca(2+)-mediated physiological process of platelets.
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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 |
Jan
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
31
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pubmed:volume |
182
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
461-5
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pubmed:dateRevised |
2005-11-17
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pubmed:meshHeading |
pubmed-meshheading:1734861-Biological Factors,
pubmed-meshheading:1734861-Blood Platelets,
pubmed-meshheading:1734861-Calpain,
pubmed-meshheading:1734861-Chromatography, Gel,
pubmed-meshheading:1734861-Chromatography, Ion Exchange,
pubmed-meshheading:1734861-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1734861-Enzyme Activation,
pubmed-meshheading:1734861-Humans,
pubmed-meshheading:1734861-Kinetics,
pubmed-meshheading:1734861-Molecular Weight
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pubmed:year |
1992
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pubmed:articleTitle |
Purification and characterization of a calpain activator from human platelets.
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pubmed:affiliation |
Dept. of Surgery II, Osaka University Medical School, Japan.
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pubmed:publicationType |
Journal Article
|