Abstract

The alcohol dehydrogenase prepared from apple (Malus domestica Borkh.) possesses both NADH and NADPH-linked activities, when assayed with acetaldehyde as substrate. The pyridine nucleotides bind to the same catalytic site on the enzyme. The alcohol dehydrogenase can also catalyse the reduction of C3–C6 aldehydes with either NADH or NADPH as cofactor.

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