Results 291 to 300 of about 502,571 (335)

Identification of Pig Brain Aldehyde Reductases with the High‐Km Aldehyde Reductase, the Low‐Km Aldehyde Reductase and Aldose Reductase, Carbonyl Reductase, and Succinic Semialdehyde Reductase

Journal of Neurochemistry, 1985
Abstract: Four NADPH‐dependent aldehyde reductases (ALRs) isolated from pig brain have been characterized with respect to substrate specificity, inhibition by drugs, and immunological criteria. The major enzyme, ALR1, is identical in these respects with the high‐Km aldehyde reductase, glucuronate reductase, and tissue‐specific, e.g., pig kidney ...
J A Cromlish, T G Flynn
openaire   +3 more sources

Nitrate reductase and cytochrome bnitrate reductase structural genes as parts of the nitrate reductase operon

Molecular and General Genetics MGG, 1981
The existence of a nitrate-reductase operon in the tryptophane region was deduced from the effects of prophage insertion in each of chlI and chlC genes and from transposition of the Mu-mediated host DNA fragments of F-prime. This operon appears to be polarized from chlC to chlI and the gene order in the region is trp -- chlI -- chlC -- purB.
Violaine Bonnefoy-Orth, Marc Chippaux, Marie-Claire Pascal, Michèle Lepelletier   +3 more
openaire   +3 more sources

NADH-Ferric Reductase Activity Associated with Dihydropteridine Reductase

Biochemical and Biophysical Research Communications, 2000
In mammals dietary ferric iron is reduced to ferrous iron for more efficient absorption by the intestine. Analysis of a pig duodenal membrane fraction revealed two NADH-dependent ferric reductase activities, one associated with a b-type cytochrome and the other not.
Andrew R. Cross, Carol Halloran, Pauline Lee, Ernest Beutler   +3 more
openaire   +3 more sources

Steroid 5 alpha-reductase: two genes/two enzymes.

Annual Review of Biochemistry, 1994
BIOCHEMICAL PROPERTIES OF STEROID Sa-REDUCTASE . . . . . . . . . . . . 30 Protein Structure . . . . . . . . . . . . . . .. . . . . . . . . . . . . . . . . . . . . . . . . 30 pH Optima . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
D. Russell, Jean D. Wilson
semanticscholar   +1 more source

Functional domains of assimilatory nitrate reductases and nitrite reductases

Trends in Biochemical Sciences, 1990
Biochemical investigation of nitrate assimilation enzymes spans the past four decades. With the molecular cloning of genes for nitrate reductases and nitrite reductases, exciting new prospects are developing for the study of these enzymes. As large, complex enzymes with multiple redox centers, these two types of reductases should help us gain ...
Wilbur H. Campbell, James R. Kinghorn
openaire   +3 more sources

Quinone Reductases

2010
Quinone reductases are a large group of enzymes that catalyze the reduction of quinones. NQO1 and NQO2 are the major mammalian quinone reductases that catalyze the reduction of quinones to hydroquinones. Both NQO1 and NQO2 are FAD-containing homodimers with a similar catalytic mechanism and overlapping substrate specificities; however, major ...
D. Siegel, D. Ross
openaire   +3 more sources

Determination of glutathione and glutathione disulfide using glutathione reductase and 2-vinylpyridine.

Analytical Biochemistry, 1980
O. Griffith
semanticscholar   +1 more source

The presence of glutathione and glutathione reductase in chloroplasts: A proposed role in ascorbic acid metabolism

Planta, 2004
C. Foyer, B. Halliwell
semanticscholar   +1 more source

The Aldose Reductase Controversy

Diabetes, 1994
ext to the debate as to whether chronic hyperglycemia is the primary cause of the late vascular complications of diabetes, the longest running controversy among researchers and clinicians studying this disease is the role of the sorbitol pathway, particularly its initial enzymatic step, the reduction of glucose to sorbitol by aldose reductase in the ...
openaire   +3 more sources

The role of glutathione reductase and related enzymes on cellular redox homoeostasis network.

Free Radical Biology & Medicine, 2016
Narciso Couto, J. Wood, J. Barber
semanticscholar   +1 more source