Linked Life Data

7002222

Source:http://linkedlifedata.com/resource/pubmed/id/7002222

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1981-2-19
pubmed:abstractText
A detailed analysis of mammalian cell surface proteins is described by a new two-dimensional polyacrylamide gel electrophoresis technique. The first dimension gel contains 2% acrylamide, 0.1% sodium dodecyl sulfate, 0.3% Triton CF10 and 9 M urea. A combination of the detergents and urea permits the separation of poorly soluble, hydrophobic cell surface proteins. Under these conditions, the molecular size of proteins has a limited contribution to the fianl separation due to a low acrylamide concentration. Differences in charge properties, hydrophobicity, and glycosylation are the elements determining the resolution. In the second dimension, the proteins are separated primarily according to molecular weights, by a conventional polyacrylamide gel system in the presence of 0.1% sodium dodecyl sulfate. In this study, proteins of C6 rat glioma cell line are characterized. Cell surface proteins are specifically radio-labeled with 125I by a lactoperoxidase method, and compared with presumptive integral surface proteins which are resistant to extraction with 0.1 M NaOH. Also studied are total cellular proteins, fucose- and glucosamine-containing glycoproteins, and protein species with variable susceptibility to weak trypsin digestion. The electrophoresis system allows an unambiguous identification of each protein species.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
625
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
179-92
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
A two-dimensional polyacrylamide gel electrophoresis system for the analysis of mammalian cell surface proteins.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't