Characterization of two D-beta-hydroxybutyrate dehydrogenase populations in heavy and light mitochondria from jerboa (Jaculus orientalis) liver. - Université de Bourgogne Accéder directement au contenu
Article Dans Une Revue Comparative Biochemistry and Physiology - Part B: Biochemistry and Molecular Biology Année : 2006

Characterization of two D-beta-hydroxybutyrate dehydrogenase populations in heavy and light mitochondria from jerboa (Jaculus orientalis) liver.

Résumé

Mitochondrial membrane-bound and phospholipid-dependent D-beta-hydroxybutyrate dehydrogenase (BDH) (EC 1.1.1.30), a ketone body converting enzyme in mitochondria, has been studied in two populations of mitochondria (heavy and light) of jerboa (Jaculus orientalis) liver. The results reveal significant differences between the BDH of the two mitochondrial populations in terms of protein expression, kinetic parameters and physico-chemical properties. These results suggest that the beta-hydroxybutyrate dehydrogenases from heavy and light mitochondria are isoform variants. These differences in BDH distribution could be the consequence of cell changes in the lipid composition of the inner mitochondrial membrane of heavy and light mitochondria. These changes could modify both BDH insertion and BDH lipid-dependent catalytic properties.
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hal-00376279 , version 1 (17-04-2009)

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Driss Mountassif, Mostafa Kabine, Norbert Latruffe, M'Hammed Saïd El Kebbaj. Characterization of two D-beta-hydroxybutyrate dehydrogenase populations in heavy and light mitochondria from jerboa (Jaculus orientalis) liver.. Comparative Biochemistry and Physiology - Part B: Biochemistry and Molecular Biology, 2006, 143 (3), pp.285-93. ⟨10.1016/j.cbpb.2005.11.019⟩. ⟨hal-00376279⟩

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