Abstract
The presence of many bands in preparations of rat liver and yeast mitochondrial structural proteins (MSP) is shown by disc (discontinuous) electrophoresis in acrylamide gel at pH 3.3 and at pH 9.9. This resolution is better than in previously reported acidic systems and is shown for the first time in a basic system. Purification of MSP with methanol – trichloroacetic acid and 8 M urea did not change the patterns except for the removal of fast-moving minor bands detectable at pH 3.3 in preparations from rat liver mitochondria.
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