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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
1976-11-1
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pubmed:abstractText |
Carboxypeptidase N has been purified 865-fold from pig serum. The enzyme has a molecular weight of approximately 315 000. In the presence of dodecylsulfate and mercaptoethanol, it dissociates into three subunits of Mr = 90 000, 50 000, 30 000, respectively. The native enzyme and the subunit of Mr = 90 000 contain carbohydrate; no carbohydrate is found in the subunits of Mr = 50 000 and 30 000. Trypsin transforms carboxypeptidase N into a form having a smaller molecular weight and enhanced activity.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jun
|
pubmed:issn |
0018-4888
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
357
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
867-72
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pubmed:dateRevised |
2009-10-27
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pubmed:meshHeading |
pubmed-meshheading:955578-Amino Acids,
pubmed-meshheading:955578-Animals,
pubmed-meshheading:955578-Carboxypeptidases,
pubmed-meshheading:955578-Chromatography, Gel,
pubmed-meshheading:955578-Kinetics,
pubmed-meshheading:955578-Metalloproteins,
pubmed-meshheading:955578-Molecular Weight,
pubmed-meshheading:955578-Swine
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pubmed:year |
1976
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pubmed:articleTitle |
Carboxypeptidase N from pig serum.
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pubmed:publicationType |
Journal Article
|