1.
Prog Clin Biol Res
; 366: 579-83, 1991.
Artigo
em Inglês
| MEDLINE
| ID: mdl-2068176
Assuntos
Catecolaminas/urina , Neuroblastoma/diagnóstico , Cromatografia Líquida de Alta Pressão/métodos , Cromatografia em Camada Fina/métodos , Ácido Homovanílico/urina , Humanos , Lactente , Programas de Rastreamento/métodos , Neuroblastoma/prevenção & controle , Neuroblastoma/terapia , Neuroblastoma/urina , Prognóstico , Ácido Vanilmandélico/urina
2.
Anal Biochem
; 121(1): 10-6, 1982 Mar 15.
Artigo
em Inglês
| MEDLINE
| ID: mdl-7091669
3.
Biochim Biophys Acta
; 566(1): 152-6, 1979 Jan 12.
Artigo
em Inglês
| MEDLINE
| ID: mdl-758955
RESUMO
Phosphate-dependent glutaminase (L-glutamine amidohydrolase, EC 3.5.1.2) from rat liver was found to be strongly activated by phosphoribosylpyrophosphate (P-rib-PP), the substrate of amidophosphoribosyltransferase (EC 2.4.2.14). Since the assay of the latter is based on the P-rib-PP-dependent conversion of glutamine to glutamate, the amidotransferase activities determined in crude tissue preparations were found to be too high. The interference of glutaminase, however, could be completely eliminated by its inactivation at 50 degrees C. Amidotransferase was not affected by the heat treatment. Because of the increased rate of the glutamate formation at this temperature, the incubation time of the assay could be significantly reduced.