Results 131 to 140 of about 8,934 (160)

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, C, Cherrier, R, Raval, R, Gay   +3 more
openaire   +2 more sources

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
openaire   +2 more sources

Purification and resolution of NADH diaphorase activity from NADPH diaphorase-linked: O2 oxidoreductase activity of human neutrophils

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
openaire   +2 more sources

Continuous monitoring of reactions that produce NADH and NADPH using immobilized luciferase and oxidoreductases from Beneckea harveyi

Analytical Biochemistry, 1978
Abstract Highly purified NADH and NADPH:FMN oxidoreductase and luciferase isolated from Beneckea harveyi have been immobilized to arylamine glass beads which were cemented to glass rods. The immobilized enzyme rods are stable, reuseable, and specific for either NADH or NADPH.
C, Haggerty, E, Jablonski, L, Stav, M, DeLuca   +3 more
openaire   +2 more sources

Interaction with arginine 597 of NADPH-cytochrome P-450 oxidoreductase is a primary source of the uniform binding energy used to discriminate between NADPH and NADH

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
openaire   +2 more sources

Studies on the NADH and NADPH: Riboflavin 5′-phosphate (FMN) oxidoreductases from Beneckea harveyi: Characterization of the FMN binding sites

Archives of Biochemistry and Biophysics, 1982
Abstract Various flavin analogs were used as alternate substrates or competitive inhibitors to characterize the FMN binding sites of the NADH- and NADPH-specific FMN oxidoreductases from Beneckea harveyi . Several polyhydroxyl compounds were found to be poor competitive inhibitors for the FMN sites of these enzymes.
B, Nefsky, M, DeLuca
openaire   +2 more sources

Subcellular location of hypothalamic progesterone metabolizing enzymes and evidence for distinct NADH- and NADHP-linked 3α-hydroxysteroid oxidoreductase activities

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
openaire   +2 more sources

[Study of the NADH and NADPH-ferredoxin oxidoreductase activities in Clostridium acetobutylicum].

Canadian journal of microbiology, 1977
The 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, C, Cherrier, J M, Bengone, R, Gay   +3 more
openaire   +1 more source

NADPH homeostasis in cancer: functions, mechanisms and therapeutic implications

Signal Transduction and Targeted Therapy, 2020
Huai-Qiang Ju, Dan Xie, Rui-Hua Xu
exaly  

Reactive oxygen species (ROS) as pleiotropic physiological signalling agents

Nature Reviews Molecular Cell Biology, 2020
Helmut Sies, Dean P Jones
exaly