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- W1236859780 abstract "This chapter describes the assay, purification, and properties of L-glutamate dehydrogenase. Frog-liver glutamate dehydrogenase can be conveniently prepared in crystalline form. The frog-liver enzyme is prepared from a mitochondrial fraction by solubilizing with detergent and fractionating and crystallizing with ammonium sulfate. After three recrystallizations, the enzyme is pure on the basis of polyacrylamide-gel electrophoresis and sedimentation experiments. The tadpole-liver enzyme has been purified several fold (specific activity equal to that of pure frog-liver enzyme) when a similar procedure is combined with chromatography on diethylaminoethyl (DEAE)-Sephadex. The rate of oxidation of diphosphopyridine nucleotide (DPNH) is measured spectrophotometrically at 340 mμ. The frog-liver enzyme is stable for several months when stored at 4° as a crystalline suspension. Many mono- and dicarboxylic L-amino acids are oxidized at significant rates by frog-liver glutamate dehydrogenase when dinitrophenyl (DPN) is the coenzyme. Adenosine diphosphate (ADP) and adenosine triphosphate (ATP) increase the rate of DPN reduction. ADP also has a similar effect on the rate of DPNH oxidation." @default.
- W1236859780 created "2016-06-24" @default.
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- W1236859780 date "1970-01-01" @default.
- W1236859780 modified "2023-10-16" @default.
- W1236859780 title "[117] l-glutamate dehydrogenase (frog and tadpole liver)" @default.
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- W1236859780 doi "https://doi.org/10.1016/0076-6879(71)17292-8" @default.
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