Immunolocalization of cholesterol side-chain-cleavage cytochrome P-450 and 17 -hydroxylase cytochrome P-450 in bovine ovarian follicles
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چکیده
منابع مشابه
Cytochrome P-450 from Bovine Adrenocortical Mitochondria: an Enzyme for the Side Chain Cleavage of Cholesterol
One cytochrome P-450 has been purified from bovine adrenocortical mitochondria to near homogeneity. The enzyme catalyzes the conversion of cholesterol and 20~ hydroxycholesterol to pregnenolone (side chain cleavage) and shows traces of 11/3-hydroxylase activity. The conversion of cholesterol to pregnenolone occurs without demonstrable accumulation of biosynthetic intermediates, i.e. hydroxylate...
متن کاملCytochrome P-450 from Bovine Adrenocortical Mitochondria: an Enzyme for the Side Chain Cleavage of Cholesterol
One cytochrome P-450 has been purified from bovine adrenocortical mitochondria to near homogeneity. The enzyme catalyzes the conversion of cholesterol and 20~ hydroxycholesterol to pregnenolone (side chain cleavage) and shows traces of 11/3-hydroxylase activity. The conversion of cholesterol to pregnenolone occurs without demonstrable accumulation of biosynthetic intermediates, i.e. hydroxylate...
متن کاملRegulation of intramitochondrial cholesterol transfer to side-chain cleavage cytochrome P-450 in rat adrenal gland.
Rat adrenal mitochondria accumulated cholesterol during ether stress in vivo when side-chain cleavage was inhibited by aminoglutethimide (control = 14.6 vs. aminoglutethimide = 26.5 micrograms of cholesterol per mg of protein). This accumulation was insensitive to simultaneous administration of cycloheximide (24.2 micrograms/mg), but side chain cleavage in the mitochondria was greatly decreased...
متن کاملInduction of synthesis of cholesterol side chain cleavage cytochrome P-450 by adrenocorticotropin in cultured bovine adrenocortical cells.
The long-term action of adrenocorticotropin (ACTH) to stimulate side chain cleavage of cholesterol has been studied utilizing confluent monolayer cultures of adult bovine adrenal cortex cells maintained for periods of time up to 72 h in the absence or presence of ACTH (lo-’ M). Following incorporation of [36S]methionine into cellular protein at various times after ACTH addition, cholesterol sid...
متن کاملCytochrome P-450 from bovine adrenocortical mitochondria: an enzyme for the side chain cleavage of cholesterol. I. Purification and properties.
One cytochrome P-450 has been purified from bovine adrenocortical mitochondria to near homogeneity. The enzyme catalyzes the conversion of cholesterol and 20~ hydroxycholesterol to pregnenolone (side chain cleavage) and shows traces of 11/3-hydroxylase activity. The conversion of cholesterol to pregnenolone occurs without demonstrable accumulation of biosynthetic intermediates, i.e. hydroxylate...
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ژورنال
عنوان ژورنال: Reproduction
سال: 1986
ISSN: 1470-1626,1741-7899
DOI: 10.1530/jrf.0.0780627