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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
|
pubmed:dateCreated |
1978-10-18
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pubmed:abstractText |
Three extracellular cellulases have been purified from cultures of Cellulomonas. One was found in solution in the cell-free supernatant and two others were found to be bound to the cellulose added as a carbon source. The free enzyme and one of the cellulose-bound enzymes bind to Sephadex. The two cellulose-bound enzymes are glycosylated. The three enzymes behave as endocellulases towards soluble carboxymethyl-cellulose and have little activity on cellulose powder.
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pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
87
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
525-31
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:98328-Actinomycetales,
pubmed-meshheading:98328-Cellulase,
pubmed-meshheading:98328-Cellulose,
pubmed-meshheading:98328-Chromatography, Gel,
pubmed-meshheading:98328-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:98328-Hydrolysis,
pubmed-meshheading:98328-Isoenzymes,
pubmed-meshheading:98328-Kinetics
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pubmed:year |
1978
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pubmed:articleTitle |
Purification and partial characterization of three extracellular cellulases from Cellulomonas sp.
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pubmed:publicationType |
Journal Article
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