Abstract
Sodium dodecyl sulfate and mercaptoethanol quantitatively solubilized delipidated bovine brain proteins and glycoproteins. Chromatography on Sepharose 4-B gave three distinct peaks. Each of the peaks were identical with respect to their amino acid composition and disc-gel electrophoresis pattern. When one of the peaks was rechromatographed on the same column it redistributed to give the same three peaks, each of which were identical by amino acid composition and disc-gel pattern. It is concluded that sodium dodecyl sulfate can solubilize but not dissociate brain proteins and glycoproteins. It is suggested that membrane proteins and other water-insoluble proteins may drastically differ from water-soluble proteins in their resistance to dissociating reagents and that molecular weights of membrane proteins obtained by sodium dodecyl sulfate electrophoresis may give erroneous results.
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