The regulation of xanthine oxidase. Inhibition by reduced nicotinamide–adenine dinucleotide of rat liver xanthine oxidase type D and of chick liver xanthine dehydrogenase

1970 ◽  
Vol 118 (5) ◽  
pp. 681.b1-681.b1
Keyword(s):  
Xanthine Oxidase ◽  
Rat Liver ◽  
Nicotinamide Adenine Dinucleotide ◽  
Xanthine Dehydrogenase ◽  
Nicotinamide Adenine ◽  
Type D ◽  
Oxidase Inhibition ◽  
Xanthine Oxidase Inhibition ◽  
Reduced Nicotinamide Adenine Dinucleotide

scholarly journals The regulation of xanthine oxidase. Inhibition by reduced nicotinamide–adenine dinucleotide of rat liver xanthine oxidase type D and of chick liver xanthine dehydrogenase

1970 ◽  
Vol 117 (1) ◽  
pp. 97-100 ◽  
Author(s):  
E. Della Corte ◽  
F. Stirpe
Keyword(s):  
Xanthine Oxidase ◽  
Rat Liver ◽  
Nicotinamide Adenine Dinucleotide ◽  
Enzyme Activities ◽  
Xanthine Dehydrogenase ◽  
Nicotinamide Adenine ◽  
Type D ◽  
Oxidase Inhibition ◽  
Xanthine Oxidase Inhibition ◽  
Reduced Nicotinamide Adenine Dinucleotide

1. Rat liver xanthine oxidase type D (NAD+-dependent) and chick liver xanthine oxidase are inhibited by NADH, which competes with NAD+. 2. The addition of a NADH-reoxidizing system in the assay of these enzyme activities is proposed. 3. Rat liver xanthine oxidase type O (oxygen-dependent) is not affected by NADH.

scholarly journals Xanthine oxidase inhibition attenuates kupffer cell production of neutrophil chemoattractant following ischemia-reperfusion in rat liver

Hepatology ◽  
1998 ◽  
Vol 28 (6) ◽  
pp. 1578-1587 ◽  
Author(s):  
Fujio Matsumura ◽  
Yasuo Yamaguchi ◽  
Mataro Goto ◽  
Osamu Ichiguchi ◽  
Eiji Akizuki ◽  
...  
Keyword(s):  
Xanthine Oxidase ◽  
Rat Liver ◽  
Kupffer Cell ◽  
Ischemia Reperfusion ◽  
Cell Production ◽  
Oxidase Inhibition ◽  
Xanthine Oxidase Inhibition

scholarly journals Coupling of uridine-5'-diphosphate (UDP) formation and nicotinamide adenine dinucleotide (NAD+) reduction for cytochemical localization of glycosyltransferases.

1983 ◽  
Vol 31 (10) ◽  
pp. 1175-1182 ◽  
Author(s):  
G R Matyas ◽  
D J Morré
Keyword(s):  
Golgi Apparatus ◽  
Rat Liver ◽  
Nicotinamide Adenine Dinucleotide ◽  
Nicotinamide Adenine ◽  
Cytochemical Localization ◽  
Permeabilized Cells ◽  
Exogenous Glucose ◽  
Dense Deposits ◽  
Donor And Acceptor ◽  
Reduced Nicotinamide Adenine Dinucleotide

A technique applicable to the cytochemical localization of glycosyltransferases through a series of coupled enzyme reactions is described. Uridine-5'-diphosphate (UDP) formed by glycosyltransferases is first phosphorylated to uridine-5'-triphosphate (UTP) by nucleoside 5'-diphosphate kinase. The UTP plus exogenous glucose-1-phosphate is converted into UDP-glucose by uridine-5'-diphosphoglucose pyrophosphorylase. UDP-glucose is then oxidized by uridine-5'-diphosphoglucose dehydrogenase to form UDP-glucuronic acid and reduced nicotinamide adenine dinucleotide (NADH). The NADH is utilized by membrane-located NADH-ferricyanide oxidoreductases in the presence of a copper salt to form electron-dense deposits of cupric ferrocyanide (Hatchett's brown). Using this technique, galactosyltransferase has been localized in cisternae (including the central midregions of the cisternae) of Golgi apparatus isolated from rat liver. Reactivity is absent from the cis-most cisternae and membrane elements. The reaction is dependent on UDP-galactose and inhibited by ethylene diaminetetraacetic acid and puromycin. the latter is a known inhibitor of galactosyltransferase of rat liver Golgi apparatus. The reaction is adaptable by varying the sugar nucleotide donor and acceptor to any glycosyltransferase utilizing UDP-sugars (except UDP-glucose). Presently it is restricted to isolated membrane fractions and permeabilized cells due to the need for accessibility of reagents and coupling enzymes.

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