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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1985-7-31
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pubmed:abstractText |
The collagenase (EC 3.4.24.3) produced by the bacterium Clostridium histolyticum has been purified free from nonspecific protease contaminants by a two-step procedure. The crude culture medium is chromatographed over heparin-Sepharose and Sephacryl S-200, and the resulting preparation has no activity versus noncollagenous proteins or N alpha-benzoyl-L-arginine ethyl ester, yet cleaves native thermally reconstituted collagen fibrils quite efficiently (specific activity, 3000 units/mg). The purification described may be useful for those investigators requiring substantially purified collagenase for applications such as cell culture or collagen quantitation in protein mixtures.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0003-2697
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
145
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
286-91
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:2990251-Arginine,
pubmed-meshheading:2990251-Centrifugation, Density Gradient,
pubmed-meshheading:2990251-Chemical Phenomena,
pubmed-meshheading:2990251-Chemistry,
pubmed-meshheading:2990251-Chromatography,
pubmed-meshheading:2990251-Clostridium,
pubmed-meshheading:2990251-Collagen,
pubmed-meshheading:2990251-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:2990251-Microbial Collagenase,
pubmed-meshheading:2990251-Peptide Hydrolases,
pubmed-meshheading:2990251-Substrate Specificity
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pubmed:year |
1985
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pubmed:articleTitle |
Purification of nonspecific protease-free collagenase from Clostridium histolyticum.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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