The Interaction of Nonionic Detergents with Protein in Paper Electrophoresis

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Abstract
Addition of polyoxyethylene nonionic detergents to the buffer in paper electrophoresis results in alteration of the rate of migration and shape of protein peaks. At low detergent concentrations, disruption of paper-protein binding leads to faster migration and sharper peaks. At high detergent concentrations, interaction of detergent with protein leads to slower migration and broader peaks. On glass-fiber paper, which binds protein less strongly than ordinary cellulose filter paper, only slowing of migration occurs upon addition of detergent to the buffer. Electrophoresis of polysaccharides using buffer-containing detergent results only in a slight increase in migration.

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