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Determination of glutamate dehydrogenase activity and its kinetics in mouse tissues using metabolic mapping (quantitative enzyme histochemistry).

Botman D, Tigchelaar W, Van Noorden CJ - J. Histochem. Cytochem. (2014)

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.

View Article: PubMed Central - PubMed

Affiliation: Department of Cell Biology and Histology, Academic Medical Center, University of Amsterdam, Amsterdam, The Netherlands (DB, WT, CJFVN).

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GDH activity in the presence of 10 mM glutamate and (A) NAD+ or (B) NADP+ as coenzyme after correction for nonspecific background staining in the absence of substrate. Activity is presented as mean Vmax ± SEM (n=3).
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fig6-0022155414549071: GDH activity in the presence of 10 mM glutamate and (A) NAD+ or (B) NADP+ as coenzyme after correction for nonspecific background staining in the absence of substrate. Activity is presented as mean Vmax ± SEM (n=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.


Determination of glutamate dehydrogenase activity and its kinetics in mouse tissues using metabolic mapping (quantitative enzyme histochemistry).

Botman D, Tigchelaar W, Van Noorden CJ - J. Histochem. Cytochem. (2014)

GDH activity in the presence of 10 mM glutamate and (A) NAD+ or (B) NADP+ as coenzyme after correction for nonspecific background staining in the absence of substrate. Activity is presented as mean Vmax ± SEM (n=3).
© Copyright Policy - open-access
Related In: Results  -  Collection

License 1 - License 2 - License 3
Show All Figures
getmorefigures.php?uid=PMC4230541&req=5

fig6-0022155414549071: GDH activity in the presence of 10 mM glutamate and (A) NAD+ or (B) NADP+ as coenzyme after correction for nonspecific background staining in the absence of substrate. Activity is presented as mean Vmax ± SEM (n=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.

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.

View Article: PubMed Central - PubMed

Affiliation: Department of Cell Biology and Histology, Academic Medical Center, University of Amsterdam, Amsterdam, The Netherlands (DB, WT, CJFVN).

Show MeSH
Related in: MedlinePlus