Evidence for the existence of a tyrosyl residue in the nicotinamide adenine dinucleotide binding site of chicken liver xanthine dehydrogenase

Biochemistry ◽  
1987 ◽  
Vol 26 (11) ◽  
pp. 3068-3072 ◽  
Author(s):  
Tomoko Nishino ◽  
Takeshi Nishino
Keyword(s):  
Binding Site ◽  
Nicotinamide Adenine Dinucleotide ◽  
Xanthine Dehydrogenase ◽  
Chicken Liver ◽  
Nicotinamide Adenine

scholarly journals Turkey liver xanthine dehydrogenase. Relation between nicotinamide-adenine dinucleotide oxidoreductase activity and the content of functional enzyme

1976 ◽  
Vol 157 (1) ◽  
pp. 283-285 ◽  
Author(s):  
I N Fhaoláin ◽  
M P Coughlan
Keyword(s):  
Methylene Blue ◽  
Nicotinamide Adenine Dinucleotide ◽  
Xanthine Dehydrogenase ◽  
Nicotinamide Adenine ◽  
Active Centre ◽  
Oxidoreductase Activity ◽  
Catalysed Oxidation

The turkey liver xanthine dehydrogenase-catalysed oxidation of NADH by Methylene Blue, by ferricyanide or by O2 is not dependent on the integrity of the active-centre persulphide groups. By contrast, the NADH-dichlorophenol-indophenol oxidoreductase and NADH-trinitrobenzenesulphonate oxidoreductase activities are directly proportional to the content of functional enzyme. These findings help to identify the sites of egress of electrons to oxidizing substrates.

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.

Effect of Niacin on Mitochondria of Allium Cepa Root Cells

1967 ◽  
Vol 25 ◽  
pp. 78-79
Author(s):  
M. Arif Hayat
Keyword(s):  
Nicotinamide Adenine Dinucleotide ◽  
Hydrogen Transfer ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Nicotinamide Adenine ◽  
Root Tips ◽  
Root Cells ◽  
Transfer Processes ◽  
Standard Procedures ◽  
A Cell ◽  
Critical Interest

Although it is recognized that niacin (pyridine-3-carboxylic acid), incorporated as the amide in nicotinamide adenine dinucleotide (NAD) or in nicotinamide adenine dinucleotide phosphate (NADP), is a cofactor in hydrogen transfer in numerous enzyme reactions in all organisms studied, virtually no information is available on the effect of this vitamin on a cell at the submicroscopic level. Since mitochondria act as sites for many hydrogen transfer processes, the possible response of mitochondria to niacin treatment is, therefore, of critical interest.Onion bulbs were placed on vials filled with double distilled water in the dark at 25°C. After two days the bulbs and newly developed root system were transferred to vials containing 0.1% niacin. Root tips were collected at ¼, ½, 1, 2, 4, and 8 hr. intervals after treatment. The tissues were fixed in glutaraldehyde-OsO4 as well as in 2% KMnO4 according to standard procedures. In both cases, the tissues were dehydrated in an acetone series and embedded in Reynolds' lead citrate for 3-10 minutes.

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