Release of Brain Mitochondrial Hexokinase by Acidic Proteins and Macromolecular Polyanions

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dc.creatorMoller, F.
dc.date2005-02-22
dc.date2005-03-22
dc.date.accessioned2026-07-07T05:58:56Z
dc.date.available2026-07-07T05:58:56Z
dc.descriptionPreparations of arachidonic acid binding and non-binding proteins from bovine brain, four acidic proteins (alpha-casein, phosvitin, beta-lactoglobulin A and B), the peptide polyglutamate, and two polyanions (heparin, dextran sulfate) enhanced both basal and glucose 6-phosphate induced solubilization of rat brain mitochondrial hexokinase (ATP:D-hexose 6-phosphotransferase, EC 2.7.1.1). In contrast, three other acidic proteins, had little (alpha-lactalbumin) or no effect (bovine serum albumin, ovalbumin) and five basic proteins inhibited release of the enzyme. Solubilizing activity therefore appears to require a net negative charge and one or more of the following structural features: extended conformation, random coil, and unordered or beta-structure, in the latter case, as the beta-barrel in the fatty acid binding proteins and beta-lactoglobulins. It is of interest that a difference of a single negative charge between beta-lactoglobulin A and B, resulted in a statistically significant difference in the stimulation of hexokinase release. Possible physiological and pathological roles of this hexokinase solubilizing effect are discussed briefly.
dc.description29 pages,3 figures. Figures and page number revised(28 pages)
dc.identifierhttps://arxiv.org/abs/q-bio/0502028
dc.identifierhttp://arxiv.org/abs/q-bio/0502028
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/88547
dc.subjectBiomolecules
dc.subjectSubcellular Processes
dc.titleRelease of Brain Mitochondrial Hexokinase by Acidic Proteins and Macromolecular Polyanions
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