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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1976-8-23
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pubmed:abstractText |
Sodium dodecyl sulfate(SDS) in a protein sample solution migrates in SDS-polyacrylamide gel electrophoresis as a band with a mobility higher than those of protein bands. Behind this band, which is mostly composed of SDS micelles, SDS concentration is raised uniformly in a gel column as a result of the retardation effect of the gel matrix on SDS micelles. Electrophoretic patterns of SDS were obtained when SDS was omitted from various portions of the gel electrophoretic system.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-924X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
78
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
349-54
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pubmed:dateRevised |
2007-12-19
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pubmed:meshHeading |
pubmed-meshheading:1228173-Binding Sites,
pubmed-meshheading:1228173-Electrodes,
pubmed-meshheading:1228173-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1228173-Indicators and Reagents,
pubmed-meshheading:1228173-Micelles,
pubmed-meshheading:1228173-Molecular Weight,
pubmed-meshheading:1228173-Proteins,
pubmed-meshheading:1228173-Sodium Dodecyl Sulfate
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pubmed:year |
1975
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pubmed:articleTitle |
Electrophoretic properties of sodium dodecyl sulfate and related changes in its concentration in SDS-polyacrylamide gel electrophoresis.
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pubmed:publicationType |
Journal Article
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