Glutamate dehydrogenase from Vicia faba

Abstract

Glutamate dehydrogenase (GDH: EC 1.4.1.2, L-glutamate: NAD+ oxidoreductase (deaminating)) from Vicia 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 seven varieties of V. faba examined possessed seven NAD-GDH isoenzymes. The number of isoenzymes remained un-changed during the germination of the variety conqueror, although there was some variation in the intensities of the bands.