par Manuel Y Keenoy, Maria Begona 
;Bodur, Hakan ;Malaisse, Willy
Référence Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology, 1118, 2, page (169-173)
Publication Publié, 1992
;Bodur, Hakan ;Malaisse, Willy Référence Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology, 1118, 2, page (169-173)
Publication Publié, 1992
Article révisé par les pairs
| Résumé : | The detritiation of L-[3-3H] alanine in the reaction catalyzed by pig heart glutamate-pyruvate transaminase was monitored in the absence or presence of lactate dehydrogenase. The results indicated that each monodirectional conversion of L-[3-3H] alanine to [3-3H] pyruvate resulted in the generation of 3HOH at a rate representing one-third of the total 3H flux. No isotopic discrimination in reaction velocity between tritiated and 14C-labelled L-alanine was observed. The mathematical modelling of the reaction revealed that, as a consequence of the detritiation process, the steady-state ratio in L-[3-3H] alanine/[3-3H] pyruvate does not inform on either the absolute or relative size of the amino acid and 2-keto acid pools. |
