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The urinary pathobiont Actinobaculum massiliense can generate androgens via the dirAB pathway. [PDF]

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Wang T   +20 more
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Regulation of the NADH and NADPH-ferredoxin oxidoreductases in Clostridia of the butyric group

Biochimica et Biophysica Acta (BBA) - General Subjects, 1976
NADH and NADPH-ferredoxin oxidoreductases have been studied in Clostridium acetobutylicum, Cl. tyrobutyricum and Cl. pasteurianum. The study of the distribution and regulation of these enzymatic activities in well-defined culture conditions, reveals that the essential function of NADPH-ferredoxin oxidoreductase is to produce NADPH, while NADH ...
H, Petitdemange   +3 more
openaire   +2 more sources

NADH(NADPH):(Acceptor) oxidoreductase activities of the bovine adrenal chromaffin granules

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1973
Abstract 1. 1. An analysis of the NADH(NADPH):(acceptor) oxidoreductase activities of adrenal chromaffin granules depleted of low molecular weight substances (notably catecholamines and ATP), has been made in terms of the flavoprotein(s) and cytochrome b 561 previously reported (Flatmark, T., Terland, O. and Helle, K. B.
O, Terland, T, Flatmark
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Purification and properties of the NADH and NADPH specific FMN oxidoreductases from Beneckea harveyi

Biochemistry, 1977
The NADH and NADPH specific FMN oxidoreductases from Beneckea harveyi have been purified to homogeneity as judged by single bands on sodium dodecyl sulfate gel electrophoresis. The overall purification for the NADH specific enzyme is 3000-fold and 4000-fold for the NADPH specific enzyme from a crude extract. The final step in the purification procedure
E, Jablonski, M, DeLuca
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Properties of the hypothalamic 5α-dihydroprogesterone NADH- and NADPH-linked 3α-hydroxysteroid oxidoreductase activities

Journal of Steroid Biochemistry, 1981
Abstract Rat hypothalamic 5α-dihydroprogesterone NADH-linked 3α-hydroxysteroid oxidoreductase, (3α-HSD) activity, which is associated with plasma membranes, has a relatively sharp pH optimum of 5.5 and a temperature optimum range of 45–52°C. This enzyme exhibited apparent K m 's for the reductive reaction of 0.40 ± 0.09 μm and 29 ± 12 μ M for ...
J E, Krause, H J, Karavolas
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