Linked Life Data

6432782

Source:http://linkedlifedata.com/resource/pubmed/id/6432782

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
1984-9-28
pubmed:abstractText
Three recombinant plasmids, pEC1, pEC2, and pEC3, each containing a unique Cellulomonas fimi chromosomal DNA insert, expressed Cm-cellulase activities in Escherichia coli C600 (Whittle, D. J., Kilburn, D. H., Warren, R. A. J., and Miller, R. C., Jr. (1982) Gene (Amst.) 17, 139-145; Gilkes, N. R., Kilburn, D. G., Langsford, M. L., Miller, R. C., Jr., Wakarchuk, W. W., Warren, R. A. J., Whittle, D. J., and Wong, W. K. R. (1984) J. Gen. Microbiol. 130, 1377-1384). Viscometric and chemical analyses showed that the enzymes encoded by pEC2 and pEC3 behaved as endoglucanases, whereas that encoded by pEC1 behaved as an exoglucanase. The activities of the exoglucanase and the pEC2-encoded endodglucanase were additive on Cm-cellulose as substrate. The pEC1-encoded enzyme also hydrolyzed xylan and p-nitrophenyl cellobioside. Two substrate-bound Cm-cellulases were isolated from the residual cellulose in a C. fimi culture by guanidine hydrochloride elution, affinity chromatography, and polyacrylamide gel electrophoresis. Both were glycoproteins of apparent Mr = 58,000 and 56,000, respectively. The 56-kDa enzyme appeared to be identical with the pEC1-encoded product, suggesting that they arise from the same gene.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
259
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10455-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Mode of action and substrate specificities of cellulases from cloned bacterial genes.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't