Carbon-13 nuclear relaxation measurements in nicotinamide adenine dinucleotide and adenosine monophosphate

1974 ◽  
Vol 96 (9) ◽  
pp. 2885-2887 ◽  
Author(s):  
W. David Hamill ◽  
Ronald J. Pugmire ◽  
David M. Grant
Keyword(s):  
Nicotinamide Adenine Dinucleotide ◽  
Adenosine Monophosphate ◽  
Nicotinamide Adenine ◽  
Nuclear Relaxation ◽  
Relaxation Measurements

FACTORS INFLUENCING TETRAZOLE REDUCTION BY REDUCED NICOTINAMIDE–ADENINE DINUCLEOTIDE IN PIGEON-HEART MITOCHONDRIA

1967 ◽  
Vol 45 (2) ◽  
pp. 299-307 ◽  
Author(s):  
C. L. Talesara ◽  
M. C. Blanchaer
Keyword(s):  
Adenosine Triphosphate ◽  
Respiratory Chain ◽  
Nicotinamide Adenine Dinucleotide ◽  
Inorganic Phosphate ◽  
Adenosine Monophosphate ◽  
Adenosine Diphosphate ◽  
Heart Mitochondria ◽  
Nicotinamide Adenine ◽  
Tetrazolium Chloride ◽  
Reduced Nicotinamide Adenine Dinucleotide

The effect of adenosine triphosphate, adenosine diphosphate, adenosine monophosphate and inorganic phosphate on the reduction of 2-(p-iodophenyi)-3-p-nitrophenyl-5-phenyl tetrazolium chloride (INT) to its formazan by reduced nicotinamide-adenine dinucleotide (NADH) was studied in pigeon-heart mitochondria. Formazan production was followed at 540 mμ in 2.2 ml medium containing 0.4–0.5 mg mitochondrial protein, 0.22 M mannitol, 0.067 M sucrose, 0.02 M Tris–chloride, 0.02 mM EDTA, 0.5–3.0 mM INT, and 38 μM NADH at pH 7.2 and 28 °C. By means of the respiratory inhibitors Amytal, rotenone, antimycin A, and cyanide, it was shown that INT diverts electrons from the respiratory chain principally at the flavoprotein level. In contrast to its inhibitory effect on "the O2-linked oxidation of NADH, 10 mM adenosine triphosphate stimulated the reaction rate and formazan yield in the present system. Equimolar inorganic phosphate also increased the initial velocity but adenosine diphosphate and adenosine monophosphate did not. Preliminary kinetic studies suggest that NADH, but not INT, combines with the form of NADH dehydrogenase in the respiratory chain with which adenosine triphosphate reacts.

Kinetic properties of glutamate dehydrogenase from the gills of Arapaima gigas and Osteoglossum bicirrhosum

1978 ◽  
Vol 56 (4) ◽  
pp. 809-813 ◽  
Author(s):  
J. H. A. Fields ◽  
W. R. Driedzic ◽  
C. J. French ◽  
P. W. Hochachka
Keyword(s):  
Glutamate Dehydrogenase ◽  
Nicotinamide Adenine Dinucleotide ◽  
Energy Charge ◽  
Adenosine Monophosphate ◽  
Adenosine Diphosphate ◽  
Nicotinamide Adenine ◽  
Kinetic Properties ◽  
Guanosine Diphosphate ◽  
Arapaima Gigas ◽  
Reduced Nicotinamide Adenine Dinucleotide

Glutamate dehydrogenase was isolated from the gills of Arapaima gigas and Osteoglossum bicirrhosum and kinetically characterized, in order to determine whether there was any alteration in the ability of the gills to generate ammonia associated with the development of an air-breathing life-style. The catalytic and regulatory properties of both enzymes were found to be very similar. They were activated by leucine, adenosine monophosphate, and adenosine diphosphate, and inhibited by guanosine triphosphate, guanosine diphosphate, and adenosine triphosphate. Inhibition by nicotinamide adenine dinucleotide and reduced nicotinamide adenine dinucleotide was strong in both cases. It was concluded that both enzymes were regulated by a combination of the energy charge of the cell and the redox potential. There is no evidence for any qualitative alteration of the gills to produce ammonia from amino acids in the air breather, Arapaima gigas, as compared with the water breather, Osteoglossum bicirrhosum.

Synthesis of nicotinamide adenine dinucleotide (NAD) from adenosine monophosphate (AMP)

1980 ◽  
Vol 102 (26) ◽  
pp. 7805-7806 ◽  
Author(s):  
David R. Walt ◽  
Victor M. Rios-Mercadillo ◽  
Jacques Auge ◽  
George M. Whitesides
Keyword(s):  
Nicotinamide Adenine Dinucleotide ◽  
Adenosine Monophosphate ◽  
Nicotinamide Adenine
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