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  • Title: Membrane potential-dependent conformational changes in mitochondrially bound hexokinase of brain.
    Author: Hashimoto M, Wilson JE.
    Journal: Arch Biochem Biophys; 2000 Dec 01; 384(1):163-73. PubMed ID: 11147827.
    Abstract:
    Previously characterized monoclonal antibodies (Mabs) were used in a study of Type I hexokinase from rat brain. Based on the relative reactivity of these Mabs with soluble and mitochondrially bound forms, binding to mitochondria was shown to affect specific epitopic regions in both N- and C-terminal halves of the enzyme and to modulate conformational changes induced by binding of the ligands, Glc or ATP. Reactivities with Mabs recognizing epitopes in two defined regions of the N-terminal half and one defined region of the C-terminal half of the mitochondrially bound enzyme were selectively affected by mitochondrial membrane potential, or by addition of oligomycin, carboxyatractyloside, or bongkrekic acid. The Glc-6-P analog, 1 ,5-anhydroglucitol-6-P, was much more effective as a competitive inhibitor against extramitochondrial ATP than against intramitochondrial ATP generated by oxidative phosphorylation. These results provide further insight into the role of hexokinase-mitochondrial interactions in regulation of cerebral glucose metabolism.
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