High impact information on diphosphopyridine nucleotide reduced

• Inclusion of NAD+ reduced the inactivation rate by manyfold, indicating the presence of -SH groups at or near the active site [1].
• The monophoton counting technique was used to obtain the fluorescence decay kinetics of NADH (dihydronicotinamide adenine dinucleotide) bound to LADH (HORSE LIVER ALCOHOL DEHYDROGENAS) [2].
• No correlation appeared to exist between the localization of neuronal DT diaphorase immunoreactivity and the dihydronicotinamide adenine dinucleotide phosphate-diaphorase-like activity, as defined by tetrazolium salt staining, used as a marker for certain peptidergic and cholinergic neurons [3].
• Intravenous infusion of 5 nmol x min(-1) x kg(-1) NAD reduced GFR and renal plasma flow (RPF) in diabetic rats but had no effect on these parameters in ND-rats [4].
• We examined the distribution of the enzyme dihydronicotinamide adenine dinucleotide phosphate-diaphorase (NADPH-d) in the superior colliculus (SC) of the New World monkey Cebus apella, and the co-localization of this enzyme with the calcium-binding proteins (CaBPs) calbindin-D28K, parvalbumin and calretinin [5].

Anatomical context of diphosphopyridine nucleotide reduced

• However, in, for example, glial cells in the cerebellum, DT diaphorase might contribute or be responsible for the histochemical dihydronicotinamide adenine dinucleotide phosphate-diaphorase activity [3].
• The relationship between NAD+ concentration and enzyme activity under initial velocity rate conditions was hyperbolic and maximum enzyme activity was seen when the NAD+ concentration was greater than 250 mumol/l. The apparent Michaelis-Menten constant (Km) was 29 mumol/l and Vmax 0.63 mumol NAD+ reduced/min/cm3 corpora lutea [6].
• Dihydronicotinamide adenine dinucleotide diaphorase in the central nervous system of the crested newt [7].
• Dihydronicotinamide adenine dinucleotide (NADH)-dependent oxidase activity in the plasma membrane of the trophoblast surface was demonstrated by cytochemical methods [8].
• With dihydronicotinamide adenine dinucleotide (NADH), we verified it was aldose reductase but not aldehyde reductase II that was activated in the erythrocytes of the patients with NIDDM [9].

Gene context of diphosphopyridine nucleotide reduced

• The mean value of kidney XDH activity was 85.41 +/- 13.81 and 46.35 +/- 6.71 mmoles NAD reduced per milligram acetone powder per hour, respectively, for the HUA and LUA lines [10].
• By using a histochemical procedure, the distribution of neurons containing dihydronicotinamide adenine dinucleotide diaphorase (NADPHd) was examined in the brain, retina and olfactory epithelium of the urodele amphibian Triturus carnifex [7].
• We show both photometrically by NADH+H+ oxidation and by HPLC product analysis that this enantiomer is rapidly reduced by NADH+H+ catalyzed by porcine heart lipoamide dehydrogenase/diaphorase [11].

Analytical, diagnostic and therapeutic context of diphosphopyridine nucleotide reduced

• EPR and spin-trapping techniques were employed to study the oxidation of the dihydronicotinamide adenine dinucleotide (NADH) photosensitized by an anthrapyrazole-antitumor agent [12].

References