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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1984-10-12
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pubmed:abstractText |
A low calcium requiring form of calcium activated neutral protease (mu-CANP) was purified to homogeneous state from a soluble fraction of human platelets. The purified protease was composed of two subunits of 80 K and 25 K proteins, judged by SDS polyacrylamide gel electrophoresis and the approximate molecular weight of 105 K was also confirmed by gel filtration technique. The purified enzyme was activated in the presence of micromolar concentration off Ca2+ and also activated with other divalent cations such as Sr2+, Ba2+, Mn2+, Ni2+. Leupeptin, antipain, an epoxysuccinate derivative (E-64), and alkylating agents were potent inhibitors of the purified enzyme.
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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
|
pubmed:month |
Jan
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pubmed:issn |
0158-5231
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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 |
71-80
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pubmed:dateRevised |
2005-11-17
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pubmed:meshHeading |
pubmed-meshheading:6089805-Blood Platelets,
pubmed-meshheading:6089805-Calpain,
pubmed-meshheading:6089805-Cations,
pubmed-meshheading:6089805-Chromatography, DEAE-Cellulose,
pubmed-meshheading:6089805-Chromatography, Gel,
pubmed-meshheading:6089805-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:6089805-Endopeptidases,
pubmed-meshheading:6089805-Humans,
pubmed-meshheading:6089805-Molecular Weight,
pubmed-meshheading:6089805-Protease Inhibitors
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pubmed:year |
1983
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pubmed:articleTitle |
Purification and characterization of a low calcium requiring form of Ca2+-activated neutral protease from human platelets.
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pubmed:publicationType |
Journal Article
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