OXIDATION OF EXTRAMITOCHONDRIAL DIPHOSPHOPYRIDINE NUCLEOTIDE BY VARIOUS TISSUES OF THE MOUSE.
Exogenous reduced diphosphopyridine nucleotide was not oxidized by mitochondria but by cytoplasmic hydrogen-accepting systems catalyzed by lactic, alpha-glycerophosphate, and malic dehydrogenases. The three enzymes were found in all tissues of the mouse; the amount of activity of each enzyme differed in the various tissues, however. It is suggested that each tissue has a unique pattern for oxidation of extramitochondrial diphosphopyridine nucleotide.
D000009:Abdominal Muscles; D000818:Animals; D001921:Brain / Q000201:enzymology*; D003964:Diaphragm; D005994:Glycerophosphates; D006321:Heart; D006801:Humans; D007668:Kidney; D007770:L-Lactate Dehydrogenase; D008099:Liver / Q000201:enzymology*; D008168:Lung; D008291:Malate Dehydrogenase; D008297:Male; D051379:Mice; D008928:Mitochondria; D009132:Muscles; D009243:NAD; D010084:Oxidation-Reduction; D010088:Oxidoreductases; D012106:Research; D013053:Spectrophotometry; D013154:Spleen; D013737:Testis
D005994:Glycerophosphates; D009243:NAD; C029620:alpha-glycerophosphoric acid; D010088:Oxidoreductases; D007770:L-Lactate Dehydrogenase; D008291:Malate Dehydrogenase
BRAIN ENZYMOLOGY; DIAPHRAGM; EXPERIMENTAL LAB STUDY; GLYCEROPHOSPHATES; HEART; KIDNEY; LACTATE DEHYDROGENASE; LIVER ENZYMOLOGY; LUNG; MALATE DEHYDROGENASE; MICE; MITOCHONDRIA; MUSCLES; NAD; OXIDOREDUCTASES; SPECTROPHOTOMETRY; SPLEEN; TESTIS