Summary: Two isoenzymes of glutamate dehydrogenase located in the cytoplasmic fraction of were specific for NAD and NADP, respectively. The NAD-dependent enzyme functioned in both directions, i.e. amination and deamination, whereas the NADP enzyme was primarily for the amination of 2-oxoglutarate to glutamate. The NADP enzyme was purified 52-fold (free of the NAD enzyme) by affinity chromatography on 2′,5′-ADP Sepharose 4B, and some of its properties studied. Substrate activation of the amination reaction of the NADP enzyme was observed with NH and NADPH. A comparison is made of the properties of the purified NADP enzyme from and . The possible roles of two isoenzymes of glutamate dehydrogenase in are discussed.


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