Results 101 to 110 of about 21,864 (146)
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Purification and properties of the NADH and NADPH specific FMN oxidoreductases from Beneckea harveyi
Biochemistry, 1977The 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
Marlene Deluca, M Deluca
exaly +4 more sources
Regulation of the NADH and NADPH-ferredoxin oxidoreductases in Clostridia of the butyric group
Biochimica Et Biophysica Acta - General Subjects, 1976NADH 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, R Gay
exaly +4 more sources
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 +3 more
openaire +3 more sources
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 +3 more
openaire +3 more sources
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
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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
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Saccharomyces cerevisiae NRE1 and IRC24 Encode Paralogous Benzil Oxidoreductases
microPublication Biology, 2023Irc24p is a benzil oxidoreductase encoded on chromosome IX of Saccharomyces cerevisiae . We identified a putative paralog, Nre1p, encoded 284 bp downstream. Both proteins are small, cytoplasmic, and are 52% identical (70% similar).
Brandon L. Garcia, K. Riley
semanticscholar +1 more source
Bioorganic chemistry (Print), 2022
7β-Hydroxysteroid dehydrogenases (7β-HSDHs) have attracted increasing attention due to their crucial roles in the biosynthesis of ursodeoxycholic acid (UDCA).
Bin Huang +7 more
semanticscholar +1 more source
7β-Hydroxysteroid dehydrogenases (7β-HSDHs) have attracted increasing attention due to their crucial roles in the biosynthesis of ursodeoxycholic acid (UDCA).
Bin Huang +7 more
semanticscholar +1 more source
NADH(NADPH):(Acceptor) oxidoreductase activities of the bovine adrenal chromaffin granules
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1973Abstract 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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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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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

