Abstract
Glutamate dehydrogenase [ l-glutamate: NAD(P) oxidoreductase (deaminating), EC 1.4.1.3] located in the mitochondria and able to utilize NAD, NADP, NADH or NADPH as substrate, has been purified 67-fold from Tetrahymena pyriformis. The activity with the four pyridine nucleotide substrates was catalyzed by a single enzyme as indicated by the constant association of the activities during purification and the coincidence of migration in polyacrylamide gel electrophoresis. Activity with NAD or NADH was stimulated by ADP and inhibited by GTP, Zn 2+, α-ketoglutarate, NADPH and NADH. NADH oxidation was inhibited by NH 4Cl or NaCl. Stimulation with ADP was strongly pH-dependent. Activity with NADPH was unaffected by ADP, GTP or Zn 2+ but was inhibited by NADPH and high concentrations of NH 4Cl or Nacl. The NADH- or NADPH-utilizing activity per mg protein was unaffected by a treatment of cells with chloramphenicol which caused a decrease in the specific activity of succinate dehydrogenase. The specific activity of NADH- and NADPH-utilizing activities increased coordinately by a factor of 2.7 during culture growth.
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