| Literature DB >> 14163795 |
Abstract
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.Entities:
Keywords: BRAIN ENZYMOLOGY; DIAPHRAGM; EXPERIMENTAL LAB STUDY; GLYCEROPHOSPHATES; HEART; KIDNEY; LACTATE DEHYDROGENASE; LIVER ENZYMOLOGY; LUNG; MALATE DEHYDROGENASE; MICE; MITOCHONDRIA; MUSCLES; NAD; OXIDOREDUCTASES; SPECTROPHOTOMETRY; SPLEEN; TESTIS
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Year: 1964 PMID： 14163795 DOI： 10.1126/science.145.3632.606
Source DB: PubMed Journal: Science ISSN： 0036-8075 Impact factor: 47.728