Abstract
An effective method, based on the chromatography on ω-aminooctyl Sepharose 4B, for the purification of the alkane-induced cytochrome P-450 is described. The purified cytochrome P-450 was homogeneous in SDS/polyacrylamide gel electrophoresis. In the oxidized state it showed a low spin type absorption spectrum. The reduced CO-complex is characterized by a Soret peak at 447 nm. The alkane hydroxylating enzyme system could be reconstituted combining purified cytochrome P-450 with partially purified NADPH-cytochrome P-450 reductase from the yeast microsomal fraction.
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Schedule a callMore From: Biochemical and Biophysical Research Communications
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