Linked Life Data

2525114

Source:http://linkedlifedata.com/resource/pubmed/id/2525114

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1989-7-18
pubmed:abstractText
We isolated a glucan-binding domain of water-insoluble glucan synthase (GTF-I) of Streptococcus sobrinus B13. Mild trypsin digestion of GTF-I bound to a water-insoluble glucan (IG) produced one predominant large fragment (55 kilodaltons). The fragment was easily recovered in IG precipitate. The isolated fragment had the same degree of affinity to IG as did the native GTF-I but no glucan synthesis activity. By the same method, a similar 55-kilodalton fragment was protected for GTF-Sd but not for GTF-Si. Immunological comparisons using specific antisera against the purified glucan-binding fragment of GTF-I from strain B13 indicated that GTF-I and GTF-S have a distinct glucan-binding domain.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0019-9567
pubmed:author
pubmed:issnType
Print
pubmed:volume
57
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2210-3
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Glucan-binding domain of a glucosyltransferase from Streptococcus sobrinus: isolation of a 55-kilodalton peptide from a trypsin digest of glucosyltransferase prebound to insoluble glucan.
pubmed:affiliation
Central Research Laboratory, Godo Shusei Co., Ltd., Chiba, Japan.
pubmed:publicationType
Journal Article