par Rasschaert, Joanne 
;Malaisse, Willy
Référence Cell biochemistry and function, 11, 3, page (155-158)
Publication Publié, 1993-09
;Malaisse, Willy Référence Cell biochemistry and function, 11, 3, page (155-158)
Publication Publié, 1993-09
Article révisé par les pairs
| Résumé : | Succinate dehydrogenase activity was measured in rat pancreatic islet homogenates incubated in the presence of [1,4-14C]succinate, the reaction velocity being judged through the generation of 14CO2 in the auxiliary reactions catalysed by pig heart fumarase and chicken liver NADP-malate dehydrogenase. In the presence of 1·0 mM succinate, the reaction velocity averaged 5·53 ± 0·44 pmol min−1 μg−1 islet protein. The Km for succinate was close to 0·4 mM and the enzymic activity was restricted to mitochondria. These kinetic results indicate that, under the present experimental conditions, the activity of succinate dehydrogenase does not vastly exceed that of either NAD-isocitrate dehydrogenase or the 2-ketoglutarate dehydrogenase complex, at least when the latter enzymes are activated by ADP and/or Ca2+. Nevertheless, the activity of succinate dehydrogenase is sufficient to account for the increase in O2 uptake evoked in intact islets by the monomethyl ester of succinic acid. It could become a rate-limiting step of the Krebs cycle in models of B-cell dysfunction. |
