Glutamate dehydrogenase from Vicia faba

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Abstract
Glutamate dehydrogenase (GDH; 1.4.1.2, L-glutamate:NAD+ oxidoreductase (deaminating)) from V. faba was assayed spectrophotometrically and was active with NAD+, NADH, or NADPH, but not with NADP+. The enzyme was localized in the particulate fraction. Activity on polyacrylamide gels was readily detected using NAD+ but only with a high concentration of coenzyme and prolonged incubation with NADP+. Each of the 7 varieties of V. faba examined possessed 7 NAD-GDH isoenzymes. The number of isoenzymes remained unchanged during the germination of the variety Conqueror, although there was some variation in the intensities of the bands.