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  • Title: Polyacrylamide gel electrophoresis of several proteins in the presence of sodium oligooxyethylene dodecyl ether sulfates or a commercially available analog.
    Author: Koide M, Fukuda M, Ohbu K, Watanabe Y, Hayashi Y, Takagi T.
    Journal: Anal Biochem; 1987 Jul; 164(1):150-5. PubMed ID: 2823630.
    Abstract:
    The behavior of water-soluble proteins and a typical membrane protein in polyacrylamide gel electrophoresis was studied in the presence of sodium oligooxyethylene dodecyl ether sulfates with a defined number of oxyethylene units or a commercially available analog with distribution and heterogeneity for the oxyethylene chain length and alkyl group, respectively. It was concluded that most water-soluble proteins do not interact with the anionic surfactants as long as their oxyethylene chain lengths are sufficiently long; the commercially available surfactant binds exceptionally well to beta-lactoglobulin without causing denaturation and subsequent dissociation; such surfactants are expected to solubilize membrane proteins without causing denaturation as judged from the result with Na+,K+-ATPase and are promising as new solubilizing agents for membrane proteins which enable efficient electrophoretic analysis or separation after the solubilization.
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