Substrate binding to hepatic microsomal cytochrome P-450. Influence of the microsomal membrane.
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چکیده
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High affinity binding of substrate and effector ligands to testicular microsomal cytochrome P-450.
The binding characteristics of substrate and effector ligands to testicular microsomal cytochrome P-450 (17 alpha-hydroxylase/C17-20 lyase) have been investigated by difference spectroscopy. Steroid products and their analogs induce oxygen-mediated damage of microsomal P-450 activities of cultured Leydig cells, whereas testosterone acetate protects P-450 from this damage [1]. Progesterone and 1...
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NADPH-cytochrome P-450 reductase was isolated from liver microsomes of phenobarbital-induced rats. The enzyme exhibits an apparent minimal molecular weight of 76,000 as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and contains 1 molecule each of FMN and FAD. Trypsin treatment of the reductase yields an enzyme with an apparent minimal molecular weight of 69,000 which r...
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متن کاملPurified Liver Microsomal NADPH-Cytochrome P-450 Reductase
NADPH-cytochrome P-450 reductase was isolated from liver microsomes of phenobarbital-induced rats. The enzyme exhibits an apparent minimal molecular weight of 76,000 as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and contains 1 molecule each of FMN and FAD. Trypsin treatment of the reductase yields an enzyme with an apparent minimal molecular weight of 69,000 which r...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1978
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)34774-9