Linked Life Data

7060593

Source:http://linkedlifedata.com/resource/pubmed/id/7060593

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1982-5-21
pubmed:abstractText
The major sialoglycoprotein of the human red-cell membrane, glycophorin A, contains 15 O-glycosidically linked oligosaccharides and one N-glycosidic oligosaccharide. The protein shows a decreased mobility on polyacrylamide gel electrophoresis in sodium dodecyl sulfate after neuraminidase treatment of the non-denatured protein. The molecular mechanism behind this phenomenon has been elucidated. Neuraminidase treatment of glycophorin A in intact cells or after solubilization in buffers containing Triton X-100 resulted in conversion of the predominant tetrasaccharide N-acetylneuraminosyl alpha 2-3galactosyl beta 1-3(N-acetylneuraminosyl alpha 2-6)-N-acetylgalactosamine to the trisaccharide galactosyl beta 1-3(N-acetylneuraminosyl alpha 2-6)-N-acetylgalactosamine and the disaccharide galactosyl beta 1-3-N-acetylgalactosamine. After denaturation with sodium dodecyl sulfate, Vibrio cholerae neuraminidase also liberated the N-acetylgalactosamine-bound sialic acids. Such treatment resulted in increased electrophoretic mobility. The results show that distal sialic acids linked to galactose are readily available to neuraminidase, and that their negative charge gives an increased electrophoretic mobility in polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. In contrast, most of the N-acetylgalactosamine-linked sialic acids of glycophorin A are not liberated by neuraminidase without denaturation of the substrate. Like sialic acids of complex-type oligosaccharides the decreased electrophoretic mobility caused by them is exclusively due to their mass while no significant contribution by the charge was seen.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
122
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
581-6
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Role of sialic acid in the mobility of membrane proteins containing O-linked oligosaccharides on polyacrylamide gel electrophoresis in sodium dodecyl sulfate.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't