Intracellular Distribution of Nicotinamide—Adenine Dinucleotide Phosphate-Linked Isocitrate Dehydrogenase, Fumarase and Citrate Synthase in Bovine Heart Muscle

1978 ◽  
Vol 6 (6) ◽  
pp. 1182-1183 ◽  
Author(s):  
HASMUKH R. FATANIA ◽  
K. DALZIEL
Keyword(s):  
Isocitrate Dehydrogenase ◽  
Nicotinamide Adenine Dinucleotide ◽  
Heart Muscle ◽  
Citrate Synthase ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Intracellular Distribution ◽  
Nicotinamide Adenine ◽  
Bovine Heart

scholarly journals The role of nicotinamide–adenine dinucleotide phosphate-dependent malate dehydrogenase and isocitrate dehydrogenase in the supply of reduced nicotinamide–adenine dinucleotide phosphate for steroidogenesis in the superovulated rat ovary

1970 ◽  
Vol 117 (1) ◽  
pp. 73-83 ◽  
Author(s):  
A. P. F. Flint ◽  
R. M. Denton
Keyword(s):  
Malate Dehydrogenase ◽  
Isocitrate Dehydrogenase ◽  
Nicotinamide Adenine Dinucleotide ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Nicotinamide Adenine ◽  
Tissue Homogenate ◽  
Kinetic Properties ◽  
Rat Ovary ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Effect Of Glucose

1. Superovulated rat ovary was found to contain high activities of NADP–malate dehydrogenase and NADP–isocitrate dehydrogenase. The activity of each enzyme was approximately four times that of glucose 6-phosphate dehydrogenase and equalled or exceeded the activities reported to be present in other mammalian tissues. Fractionation of a whole tissue homogenate of superovulated rat ovary indicated that both enzymes were exclusively cytoplasmic. The tissue was also found to contain pyruvate carboxylase (exclusively mitochondrial), NAD–malate dehydrogenase and aspartate aminotransferase (both mitochondrial and cytoplasmic) and ATP–citrate lyase (exclusively cytoplasmic). 2. The kinetic properties of glucose 6-phosphate dehydrogenase, NADP–malate dehydrogenase and NADP–isocitrate dehydrogenase were determined and compared with the whole-tissue concentrations of their substrates and NADPH; NADPH is a competitive inhibitor of all three enzymes. The concentrations of glucose 6-phosphate, malate and isocitrate in incubated tissue slices were raised at least tenfold by the addition of glucose to the incubation medium, from the values below to values above the respective Km values of the dehydrogenases. Glucose doubled the tissue concentration of NADPH. 3. Steroidogenesis from acetate is stimulated by glucose in slices of superovulated rat ovary incubated in vitro. It was found that this stimulatory effect of glucose can be mimicked by malate, isocitrate, lactate and pyruvate. 4. It is concluded that NADP–malate dehydrogenase or NADP–isocitrate dehydrogenase or both may play an important role in the formation of NADPH in the superovulated rat ovary. It is suggested that the stimulatory effect of glucose on steroidogenesis from acetate results from an increased rate of NADPH formation through one or both dehydrogenases, brought about by the increases in the concentrations of malate, isocitrate or both. Possible pathways involving the two enzymes are discussed.

scholarly journals The interaction of reduced nicotinamide–adenine dinucleotide phosphate with reduced nicotinamide–adenine dinucleotide–ubiquinone reductase from bovine heart mitochondria

1976 ◽  
Vol 158 (1) ◽  
pp. 149-151 ◽  
Author(s):  
C I Ragan
Keyword(s):  
Nicotinamide Adenine Dinucleotide ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Heart Mitochondria ◽  
Nicotinamide Adenine ◽  
Bovine Heart ◽  
Reduced Nicotinamide Adenine Dinucleotide

Reduction of the chromophores of mitochondrial NADH-ubiquinone reductase by NADPH reaches only 50% of the extent of reduction by NADH, monitored at 450 nm. This effect is due to autoxidation of an enzyme component at a higher rate than its reduction by NADPH.

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