魚類の六炭糖燐酸化経路に関する研究-I. : アカカマス肝臓のグルコース-6-燐酸脱水素酵素の諸性質

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The enzymatic properties of glucose-6-phosphate dehydrogenase in the liver of barracuda, Sphyraena pinguis, were investigated and the results obtained were as follows: Glucose-6-phosphate dehydrogenase was present in the liver and kidney of barracuda, yellow-tail and carp, and the existence of hexose monophosphate shunt in fish tissues was suggested by the presence of glucose-6-phosphate dehydrogenase, phosphogluconate dehydrogenase, phosphoglucose isomerase and fructose diphosphatase in these tissues. The enzyme was relatively active at pH 8.0 and was relatively stable at pH 7.0. Nicotinamide-adenine dinucleotide phosphate was necessary for the enzyme as coenzyme and the activity was activated by calcium, barium and magnesium ions and inhibited by mercuric ions. The apparent Michaelis constant was 4.5×10-5 M for glucose-6-phosphate or 2.0×10-5 M for nicotinamide-adenine dinucleotide phosphate.
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