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- W2092283573 abstract "A cytochrome P-450 which cholesterol side-chain claving activity was solubilized from beef adrenal mitochondria with sodium deoxycholate and glycerol and purified by chromatography on DEAE-Sephadex. This preparation interacts spectrally with and performs side-chain cleavage of cholesterol and 20α-hydroxycholesterol but does not react with substrates for IIβ- or 18-hydroxylation. Absolute visible and ESR spectra indicate that this preparation is an equilibrium mixture of high- and low-spin statess of P-450 Fe3+. Cholesterol binding increase the relative proportion of the high-spin form, and 20α-hydroxycholesterol increases the relative proportion of the low-spin form of the cytochrome. Kinetic studies of the enzyme's reducibility show that the rate of reduction of Fe3+ to Fe2+ is related to the proportion of high-spin P-450 present." @default.
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- W2092283573 date "1973-08-01" @default.
- W2092283573 modified "2023-10-18" @default.
- W2092283573 title "Solubilization and properties of bovine adrenal cortical cytochrome P-450 which cleaves the cholesterol side chain" @default.
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- W2092283573 doi "https://doi.org/10.1016/0005-2744(73)90259-3" @default.
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