1887

Abstract

Cell-free extracts of contained the enzymes necessary for both oxidative and non-oxidative pentose phosphate metabolism. The specific activities of these enzymes changed little during differentiation. The properties of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase were studied with respect to values for substrates and cofactor NADP. The two dehydrogenases were relatively unstable in extracts prepared from early stages of development. The value of phospho-glucose isomerase for glucose 6-phosphate was approximately 30-fold higher than that of glucose-6-phosphate dehydrogenase. Measurements of pentose phosphate pathway intermediates were made throughout development. All measured intermediates except fructose 1,6-bisphosphate appeared to accumulate between aggregation and culmination. Fructose 1,6-bisphosphate concentrations remained constant until culmination, then dropped 3-fold during sorocarp construction. Calculation of mass-action ratios for the pentose phosphate reactions suggested that glucose-6-phosphate dehydrogenase was the only reaction greatly displaced from equilibrium. These results are discussed in relation to factors controlling pentose phosphate metabolism during development in

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1979-08-01
2021-07-28
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