Purification of NADP-dependent glutamate dehydrogenase from Pseudomonas aeruginosa and immunochemical characterization of its in vivo inactivation.
Biochim Biophys Acta
; 801(1): 32-9, 1984 Sep 07.
Article
en En
| MEDLINE
| ID: mdl-6432059
ABSTRACT
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.
Search on Google
Banco de datos:
MEDLINE
Asunto principal:
Pseudomonas aeruginosa
/
Glutamato Deshidrogenasa
Idioma:
En
Año:
1984
Tipo del documento:
Article