Determination of glutamate dehydrogenase activity and its kinetics in mouse tissues using metabolic mapping (quantitative enzyme histochemistry).
Bottom Line: Glutamate dehydrogenase (GDH) catalyses the reversible conversion of glutamate into α-ketoglutarate with the concomitant reduction of NAD(P)(+) to NAD(P)H or vice versa.NAD(+)-dependent GDH V(max) was 2.5-fold higher than NADP(+)-dependent V(max), whereas the K(m) was similar, 1.92 mM versus 1.66 mM, when NAD(+) or NADP(+) was used, respectively.In all tissues, the highest activity was found when NAD(+) was used as a coenzyme.
Affiliation: Department of Cell Biology and Histology, Academic Medical Center, University of Amsterdam, Amsterdam, The Netherlands (DB, WT, CJFVN).Show MeSH
Related in: MedlinePlus
License 1 - License 2 - License 3
Mentions: GDH activity in various mouse tissues was determined with either NAD+ or NADP+ as coenzyme (Fig. 6). Liver had the highest GDH activity (at least 4.5-fold higher activity over other tissues when NAD+ was used as coenzyme and at least 3.5-fold with NADP+ as coenzyme). NADP+-dependent GDH activity was only observed in the liver and pancreas. With NAD+ used as a cofactor, activity in the cerebellum, small intestines and heart was also found.
Affiliation: Department of Cell Biology and Histology, Academic Medical Center, University of Amsterdam, Amsterdam, The Netherlands (DB, WT, CJFVN).