Abstract
NADP-dependent glutamate dehydrogenase was partially purified from extracts of the marine siphonous green alga Caulerpa simpliciuscula. The enzyme had an apparent Km NH4+ of 0.4 to 0.7 mm and was highly specific for NADPH, α-ketoglutarate, and ammonium ions.
The bulk of the NADP-glutamate dehydrogenase was isolated with the chloroplast fraction in cell-free preparations of this alga and was released from these “chloroplast fractions” as a soluble enzyme on gentle lysis of chloroplast membranes.
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