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The NADP-specific glycerol dehydrogenase of rat skeletal muscle has been partially purified by ammonium sulphate fractionation. The enzyme has been studied kinetically by initial-velocity analysis, product inhibition and inhibition by fluoride. The experimental results indicate that the reaction mechanism for the enzyme is ordered such that the first product leaves the enzyme before the addition of the second substrate.

The kinetics and reaction mechanism of the nicotinamide–adenine dinucleotide phosphate-specific glycerol dehydrogenase of rat skeletal muscle