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- W257877015 abstract "Protein-lipid interactions in the liver microsomal hydroxylase system have been studied with delipidated purified cytochrome P-450 by reconstitution with phospholipid and with binding studies with the detergent, Triton X-100. It was found that upon recombination with phospholipid, delipidated P-450 was rena-tured, a process that was followed by the increase in absorption at 450 nm of the reduced, CO-bound complex. The renaturation, measured spectrophotometrically, was correlated to an increased NaIO4-supported 6β-hydroxylation of androstenedione. In NADPH-supported 6β-hydroxylation about 100 times more phospholipid was necessary to get maximal lipid stimulation. It is suggested that the lipid has a dual function in the liver microsomal system, (A) binding to P-450 thereby inducing the active conformation of the enzyme and (B) forming a fluid environment that facilitates electron transport from NADPH to P-450. In binding studies with Triton X-100 it was found that P-450 bound its own weight in detergent thereby dissociating from a tetrameric to a monomeric form which was catalytically active in 6β-hydroxylation of androstenedione in both NaIO4 and NADPH-supported reactions." @default.
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- W257877015 date "1977-01-01" @default.
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- W257877015 title "PROTEIN-LIPID INTERACTIONS IN THE LIVER MICROSOMAL HYDROXYLASE SYSTEM" @default.
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- W257877015 doi "https://doi.org/10.1016/b978-0-08-021523-5.50016-x" @default.
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