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Estrogen synthetase in the horse
Author(s) -
Vibet A.,
Dintinger T.,
Maboundou J.C.,
Gaillard J.L.,
Divoux D.,
Silberzahn P.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80629-w
Subject(s) - agarose , biochemistry , molecular mass , horse , reductase , sepharose , cytochrome , enzyme , cytochrome c , placenta , chemistry , microbiology and biotechnology , biology , specific activity , mitochondrion , pregnancy , paleontology , fetus , genetics
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 V max and K m , suggesting that they are not species specific.