Linked Life Data

6816934

Source:http://linkedlifedata.com/resource/pubmed/id/6816934

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1983-2-14
pubmed:abstractText
Cell-bound opacity factor (OF) was extracted with sodium dodecyl sulphate (SDS) to yield stable extracts with titres of greater than 20 000. The mol.-wt distributions of extracellular and SDS-extracted OF, determined by ultrafiltration or chromatography on Sepharose 4B, suggested that the high mol. wt (1 x 10(6)) of extracellular OF is due to aggregation, because cell-bound and extracellular OF in the presence of SDS had an average mol. wt of only 2 x 10(5). At least four apparent multiple-molecular forms (mol. wt 7.4-12.0 x 10(4)) of OF were detected by SDS polyacrylamide-gel electrophoresis. It seemed more probable that these were due to aggregation rather than the existence of different stable conformations. To explain the molecular-size distribution, the subunit would have to be as small as 1 x 10(4) but this was supported by the finding that OF can be detected after passing through a dialysis membrane provided that its "substrate", alpha 1-lipoprotein, is present on the other side. This raises the possibility that OF is associated with a carrier molecule. The isoelectric-focusing profiles of OF were complex and differed markedly with the method used to prepare OF. Extracellular OF had a simple profile with an isoelectric point of 4.0, whereas Triton-extracted OF was the most complex and formed three peaks, the position of which varied depending on whether the detergent was present or absent during focusing runs.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-2615
pubmed:author
pubmed:issnType
Print
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
451-64
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
The opacity factor of group-A streptococci.
pubmed:publicationType
Journal Article