A highly purified preparation of cytochrome P-450 from microsomes of anaerobically grown yeast. |
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Authors: | Y Yoshida Y Aoyama H Kumaoka S Kubota |
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Institution: | Faculty of Pharmaceutical Sciences, Mukogawa University, Nishinomiya, Hyogo 663, Japan |
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Abstract: | Cytochrome P-450 was purified from microsomes of anaerobically grown yeast to a specific content of 12–15 nmoles per mg of protein with a yield of 10–30%. Upon sodium dodecylsulfate/polyacrylamide gel electrophoresis, the purified preparation yielded a major protein band having a molecular weight of about 51,000 together with a few faint bands. It was free from cytochrome b5, NADH-cytochrome b5 reductase, and NADPH-cytochrome c (P-450) reductase. In the oxidized state it exhibited a low-spin type absorption spectrum, and its reduced CO complex showed a Soret peak at 447–448 nm. It was reducible by NADPH in the presence of an NADPH-cytochrome c reductase preparation purified from yeast microsomes. Its conversion to the cytochrome P-420 form was much slower than that of hepatic cytochrome P-450. |
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Keywords: | DTT dithiothreitol sodium dodecylsulfate |
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