PMID: 2106448Feb 12, 1990Paper

Estrogen synthetase in the horse. Comparison of equine placental and rat liver NADPH-cytrochrome c (P-450) reductase activities

FEBS Letters
A VibetP Silberzahn

Abstract

NADPH-cytochrome c (P-450) reductases from horse placenta and rat liver were purified and their biological activities compared using cytochrome c as substrate. Rat liver reductase was purified to electrophoretic homogeneity in one chromatographic step on 2',5'-ADP agarose, and had a relative mass of 85,000 Da as estimated by SDS-PAGE. Equine placental reductase was separated from cytochrome P-450 on aminohexyl-Sepharose 4B and further purified on 2',5-ADP agarose; this preparation exhibited two bands, one of 85,000 and one of 80,000 Da, on SDS-PAGE. The lower molecular weight form was assumed to be a proteolytic product of the higher molecular weight form. A high retention of activity was obtained in both preparations. Equine placenta and rat liver enzymes were found to exhibit very similar Vmax and Km, suggesting that they are not species specific.

References

Jan 29, 1986·Biochemical and Biophysical Research Communications·S NakajinP F Hall
Oct 23, 1974·Biochemical and Biophysical Research Communications·J L Vermilion, M J Coon

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Citations

Jun 1, 1993·European Journal of Biochemistry·S MoslemiJ L Gaillard
May 9, 2007·Archives of Environmental Contamination and Toxicology·N BenachourG E Séralini
Jun 3, 2005·Environmental Health Perspectives·Sophie RichardGilles-Eric Seralini
Aug 4, 2001·Biochemical and Biophysical Research Communications·D C LambS L Kelly
Sep 1, 1996·The Journal of Steroid Biochemistry and Molecular Biology·J AlmadhidiG E Séralini
Jan 7, 1998·Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology·S MoslemiJ L Gaillard

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