2005/02/22 by F. Moller, Moller, F.
Biochemistry, Genetics and Molecular Biology · Materials Science · #Biomolecules (q-bio.BM) #Endoplasmic Reticulum Stress and Disease #Enzyme Structure and Function #FOS: Biological sciences #Protein Structure and Dynamics #Subcellular Processes (q-bio.SC) #q-bio.BM #q-bio.SC
paper · pdf · doi:10.48550/arxiv.q-bio/0502028
29 pages,3 figures. Figures and page number revised(28 pages)
openalex publication_date 2005/02/22 · arxiv created 2005/03/22 · arxiv updated 2009/12/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/28
Preparations 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.