Purification and properties of NADP-dependent glutamate dehydrogenase from yeast nuclear fractions.
1. NADP-dependent glutamate dehydrogenase (EC 1.4.1.4) extracted from nuclear fractions of Saccharomyces cerevisiae was partially purified. The final purification achieved was over 100-fold over the initial extract. 2. Cellulose acetate electrophoresis shows that the preparation is close to homogeneity and that the enzyme is slightly more anionic than cytoplasmic glutamate dehydrogenase. 3. The response of the nuclear activity to variation of pH, of inorganic phosphate and other electrolyte concentration and of the concentration of the reaction substrates has been investigated. Several differences were detected in comparison with cytoplasmic glutamate dehydrogenase.
D002467:Cell Nucleus / Q000201:enzymology*; D003593:Cytoplasm / Q000201:enzymology; D004588:Electrophoresis, Cellulose Acetate; D005969:Glutamate Dehydrogenase / Q000302:isolation & purification / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009249:NADP; D010710:Phosphates / Q000494:pharmacology; D011523:Protoplasts / Q000201:enzymology; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D014325:Tromethamine / Q000494:pharmacology
D010710:Phosphates; D014325:Tromethamine; D009249:NADP; D005969:Glutamate Dehydrogenase