Properties of yeast glutamate dehydrogenase

C. López-Quijada
43

Abstract




A method for the purification of glutamic deshidrogenase from yeast is presented. The method is very reproducible andresults in excellent yields of preparations of high specific activity which are homogeneous in the ultracentrifuge. The enzyme catalyzes at pH 7.6 the oxidation of NaADPH2>-14 times faster than the reduction of NADP. It has negligible activity with NADH2 and NAD. The enzyme is very stable perticularly in the presence of salt. However, it is more stable in the presence of NADPHa as with the glutamic deshidrogenase from liver.




Keywords:
BIOCHEMISTRY, Biochemical Phenomena, Biochemistry, GLUTAMATES, Glutamate Dehydrogenase, Glutamates, NAD, NADP, OXIDOREDUCTASES, Oxidoreductases, SACCHAROMYCES, Saccharomyces, Saccharomyces cerevisiae, Yeast, Dried

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C. López-Quijada


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