Purification of NADP-dependent glutamate dehydrogenase from Pseudomonas aeruginosa and immunochemical characterization of its in vivo inactivation.
The 'high ammonia pathway' enzyme glutamate dehydrogenase (NADP+) is inactivated in cells of Pseudomonas aeruginosa when the stationary phase of growth is reached. Purified glutamate dehydrogenase (NADP+) appeared to be a protein composed of six identical subunits with a molecular weight of 54 000. With antibodies raised against purified enzyme it was found that glutamate dehydrogenase (NADP+) inactivation is accompanied by a parallel decrease in immunologically reactive material. This suggests that glutamate dehydrogenase (NADP+) inactivation is caused or followed by rapid proteolysis.
D000936:Antigen-Antibody Complex; D003429:Cross Reactions; D005969:Glutamate Dehydrogenase / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D007106:Immune Sera; D005779:Immunodiffusion; D007700:Kinetics; D009249:NADP / Q000378:metabolism; D011550:Pseudomonas aeruginosa / Q000201:enzymology*
D000936:Antigen-Antibody Complex; D007106:Immune Sera; D009249:NADP; D005969:Glutamate Dehydrogenase