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Modulation of rabbit and human hepatic cytochrome P-450-catalyzed steroid hydroxylations by alpha-naphthoflavone.
Rifampicin induces cytochrome P-450 3c, progesterone 16 alpha- and 6 beta-hydroxylation, 17 beta-estradiol 2-hydroxylation, benzo[a] pyrene hydroxylation, and erythromycin N-demethylation in rabbitExpand
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Regulation of the rabbit cytochrome P-450 3c gene. Age-dependent expression and transcriptional activation by rifampicin.
The macrolide antibiotic rifampicin is a potent inducer of cytochrome P-450-mediated drug metabolism in humans and rabbits. In this report, we demonstrate that in immature rabbits, rifampicinExpand
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Comparison of the biochemical composition of four preparations of contracting cardiac muscle.
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Pumping tests of well Campbell et al. No. 2, Gila Hot Springs, Grant County, New Mexico
Well Campbell et al. No. 2 near Gila Hot Springs in southwestern New Mexico (Section 5, Township 13 South, Range 13 West) was pumped for a five-step test and a 48-hour constant-rate test duringExpand
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Variation in hepatic microsomal cytochrome P-450 1 concentration among untreated rabbits alters the efficiency of estradiol hydroxylation.
The metabolism of 17 beta-estradiol was examined using both rabbit liver microsomes and highly purified forms of rabbit liver microsomal cytochrome P-450. The predominant microsomal metabolite of 17Expand
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Active site-directed inhibition of rabbit cytochrome P-450 1 by amino-substituted steroids.
A variety of amino-substituted steroids were investigated as inhibitors of the rabbit hepatic, steroid 21-hydroxylase, cytochrome P-450 1. We reasoned that a steroid analog of pregnenolone capable ofExpand
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Constitutive forms of rabbit-liver microsomal cytochrome P-450: enzymatic diversity, polymorphism and allosteric regulation.
Large, independent variations occur among New Zealand White rabbits in the 21- and and 6 beta-hydroxylation of progesterone as catalysed by liver microsomes. These reactions are catalysedExpand
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Multiple forms of cytochrome P-450: catalytic differences exhibited by two homogeneous forms of rabbit cytochrome P-450.
Two highly purified forms of hepatic cytochrome P-450 were isolated from rabbits treated with the inducers phenobarbital and 2,3,7,8-tetrachlorodibenzo-p-dioxin. Both forms were shown to beExpand
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Allosteric regulation of the 16 alpha-hydroxylation of progesterone as catalyzed by rabbit microsomal cytochrome P-450 3b.
A variety of compounds that can arise from the metabolism of progesterone in vivo stimulate the 16 alpha-hydroxylation of progesterone as catalyzed by highly purified, reconstituted preparations ofExpand
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Positive effectors of the binding of an active site-directed amino steroid to rabbit cytochrome P-450 3c.
The binding of the amino steroid, 22-amino-23,24-bisnor-5-cholen-3 beta-ol (22-ABC), to rabbit liver cytochrome P-450 3c was studied using purified P-450 3c and liver microsomes prepared fromExpand
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