Results 131 to 140 of about 8,969 (152)
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Biochemistry, 1993
Site-directed mutagenesis has been used in conjunction with pH and alternate substrate/inhibitor studies to characterize the interactions between NADPH-cytochrome P-450 oxidoreductase (P-450R) and the 2'-phosphate of NADP(H) that provide P-450R with its strong nicotinamide nucleotide specificity. It is known that the 2'-phosphate of NADP(H) is bound to
D S, Sem, C B, Kasper
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Site-directed mutagenesis has been used in conjunction with pH and alternate substrate/inhibitor studies to characterize the interactions between NADPH-cytochrome P-450 oxidoreductase (P-450R) and the 2'-phosphate of NADP(H) that provide P-450R with its strong nicotinamide nucleotide specificity. It is known that the 2'-phosphate of NADP(H) is bound to
D S, Sem, C B, Kasper
openaire +2 more sources
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1985
Intrinsic NADPH diaphorase activity is a component of the membrane-bound NAD(P)H:O2 oxidoreductase of human neutrophils. NADH-specific diaphorase activity is also present in membrane fractions rich in oxidoreductase activity. Studies were undertaken to determine whether the NADH diaphorase might also be intrinsic to the oxidoreductase.
T R, Green, D E, Wu
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Intrinsic NADPH diaphorase activity is a component of the membrane-bound NAD(P)H:O2 oxidoreductase of human neutrophils. NADH-specific diaphorase activity is also present in membrane fractions rich in oxidoreductase activity. Studies were undertaken to determine whether the NADH diaphorase might also be intrinsic to the oxidoreductase.
T R, Green, D E, Wu
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Journal of Steroid Biochemistry, 1980
Abstract The subcellular location of adult female rat hypothalamic steroid 5α-reductase and 3α-hydroxysteroid oxidoreductase (3α-HSD) activities, which catalyze the conversion of progesterone to 3α-hydroxy-5α-pregnan-20-one via 5α-pregnane-3,20-dione, have been investigated using 3 H-labeled substrates and an isotopic dilution assay system. In crude
J E, Krause, H J, Karavolas
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Abstract The subcellular location of adult female rat hypothalamic steroid 5α-reductase and 3α-hydroxysteroid oxidoreductase (3α-HSD) activities, which catalyze the conversion of progesterone to 3α-hydroxy-5α-pregnan-20-one via 5α-pregnane-3,20-dione, have been investigated using 3 H-labeled substrates and an isotopic dilution assay system. In crude
J E, Krause, H J, Karavolas
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[Study of the NADH and NADPH-ferredoxin oxidoreductase activities in Clostridium acetobutylicum].
Canadian journal of microbiology, 1977The NADH and NADPH-ferredoxin oxidoreductase have been studied in Clostridium acetobutylicum. Acetyl-CoA is an obligatory activator of NADH-ferredoxin reductase activity and NADH a competitive inhibitor of ferredoxin-NAD+ reductase activity. These regulations are the same when C.
H, Petitdemange +3 more
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Development of a Thioredoxin‐Based Cofactor Regeneration System for NADPH‐Dependent Oxidoreductases
ChemCatChem, 2022Ningning Zhang +2 more
exaly

