Abstract
NADH-cytochrome b 5 reductase has been solubilized by extraction of rabbit liver microsomes with 1 m potassium phosphate buffer (pH 7.4), and has been purified to comparable purity with the Triton X-100-solubilized enzyme. Gel electrophoresis indicated an apparent molecular weight of 33,000 for both phosphate buffer-extracted and Triton X-100-solubilized enzymes. Phosphate buffer extraction provides a simple mild procedure for the extraction of NADH-cytochrome b 5 reductase that avoids detergents or proteolytic agents.
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