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The kinetics of the reaction of NADP+-specific isocitrate dehydrogenase was examined by using the enzyme purified from the pupae of silkworm, Bombyx mori. The binding of the individual substrates, isocitrate and NADP+, depended upon each other, and was competitive with the reaction products, CO" cu-ketoglutarate and NADPH. The mechanism appears to be of a rapid equilibrium random type. These findings were very similar to those reported for NADP+-specific isocitrate dehydrogenases isolated fromdoi:10.5109/23653 fatcat:mdwxiunmbvekhnlfjbm6qpoqpi