Purification of NADP-dependent glutamate dehydrogenase from Pseudomonas aeruginosa and immunochemical characterization of its in vivo inactivation |
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| Authors: | Rob AMM Smits Frank R Pieper Chris van der Drift |
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| Institution: | Department of Microbiology, Faculty of Science, University of Nijmegen, Toernooveld, NL-6525 ED Nijmegen The Netherlands |
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| Abstract: | The ‘high ammonia pathway’ enzyme glutamate dehydrogenase (NADP+) is inactivated in cells of Pseudomonas aeruginosa when the stationary phase of growth in 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. |
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| Keywords: | NADP Glutamate dehydrogenase Enzyme inactivation (P aeruginosa) |
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