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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:dateCreated |
1987-5-13
|
| pubmed:abstractText |
A simple method of purification for the extracellular D-glucosyltransferase (GTase) from a serotype c strain Streptococcus mutans was developed using chromatography on DEAE-Sephacel and CM-cellulose. The GTase had a molecular weight of 155,000 and an isoelectric point of 7.4. The enzyme converted sucrose, in the absence of dextran T-10, into a branched (1----6)-linked alpha-D-glucan having some alpha-(1----3)-linked D-glucosyl residues. The GTase was similar to GTases which have been isolated from other strains of serotype c S. mutans and which synthesise water-soluble glucans. In addition, the amino acid composition of the GTase protein was relatively similar to those of the GTases from serotype g S. mutans which synthesise water-soluble and water-insoluble glucans.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Dec
|
| pubmed:issn |
0008-6215
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
158
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
147-55
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| pubmed:dateRevised |
2000-12-18
|
| pubmed:meshHeading | |
| pubmed:year |
1986
|
| pubmed:articleTitle |
Purification and characterisation of the extracellular D-glucosyltransferase from serotype c Streptococcus mutans.
|
| pubmed:publicationType |
Journal Article
|