Results 121 to 130 of about 78,380 (148)

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

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

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

Stereospecificity of Hydrogen Transfer by Fungal and Plant NADPH:Isoflavone Oxidoreductases

Phytochemistry, 1990
Wolfgang Barz, Dittmar Schlieper
exaly  

Crystal Structure ofEscherichia coliQOR Quinone Oxidoreductase Complexed With NADPH

Journal of Molecular Biology, 1995
Nicholas E. Dixon, David Ollis, D L Ollis   +2 more
exaly  

Synthesis of 4R- and 4S-Tritium Labeled NADPH for the Determination of the Coenzyme Stereospecificity of NADPH: Protochlorophyllide Oxidoreductase

Biochemical and Biophysical Research Communications, 1987
W R Richards
exaly  

[THE ENZYMATIC REGULATION AT THE LACTATE OXIDOREDUCTASE LEVEL. NADH AND NADPH OXIDASES AS WELL AS NADP REACTIVE LACTATE OXIDOREDUCTASE IN RED BLOOD CELLS].

Acta biologica et medica Germanica, 1996
S, RAPOPORT, L, ABABEI
openaire   +1 more source