Linked Life Data

1125324

Source:http://linkedlifedata.com/resource/pubmed/id/1125324

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1975-8-4
pubmed:abstractText
The in vivo incorporation of [35-S]sulfate and [3H]fucose into rat brain myelin was investigatedmmost of the 35S in the myelin was in sulfatide, but about 4% was associated with the residual proteins after chloroform/methanol extraction. Polyacrylamide gel electrophoresis of these proteins indicated that the major 35-S-labeled component corresponded to the major fucose-labeled glycoproteinmthe labeling of this predominant glycoprotein with sulfate was more selective than with fucose, since there was relatively little incorporation of sulfate into some of the minor fucose-labeled glycoproteins. There was little or no 35-S associated with proteolipid or basic protein on polyacrylamide gels. The fucose-labeled glycoproteins were converted to glycopeptides by pronase digestion and separated into two major classes by gel filtration on Sephadex-G-50. Only the higher molecular weight class contained significant amounts of 35-S. The association of 35-S with the glycopeptides was not due to binding of sulfatide or free inorganic sulfate. The results indicate that the predominant myelin-associated glycoprotein in rat brain is sulfated.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
392
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
159-66
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1975
pubmed:articleTitle
[35-S]sulfate incorporation into myelin glycoproteinsmi=entral nervous system.
pubmed:publicationType
Journal Article