This report describes a new method of disc electrophoresis for strongly basic proteins using arginine-acetate buffer at pH 9.0 as a tray buffer. The electrophoretic patterns of various basic proteins (i. e., HML, EWL, cytochrome C and histone) were studied and compared with acidic and alkaline conditions. As to lysozymes, the mixture of HML and EWL, clearly separated into two discs under the alkaline condition although the electrophoretic mobilities of both lysozymes under acidic condition were identical or not significantly different. Cytochrome C, which exhibited a main brown disc under acidic condition, divided into two discs with brown color due to ferric ion. In histone, 7 discs that were detected in acidic condition separated into at least 15 discs under the alkaline condition.
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