淡江大學機構典藏:Item 987654321/61852
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    Please use this identifier to cite or link to this item: https://tkuir.lib.tku.edu.tw/dspace/handle/987654321/61852


    Title: Evidence for mitochondrial localization of betaine aldehyde dehydrogenase in rat liver - purification, characterization and comparison with human cytoplasmic E3 isozyme
    Authors: Chern, Ming-kai;Pietruszko, Regina
    Contributors: 淡江大學生命科學研究所
    Keywords: Aldehyde;Betaine;Dehydrogenase;Mitochondria;Rat liver
    Date: 1999-06
    Issue Date: 2013-05-31 11:33:29 (UTC+8)
    Publisher: Ottawa: NRC Research Press
    Abstract: Betaine aldehyde dehydrogenase has been purified to homogeneity from rat liver mitochondria. The properties of betaine aldehyde dehydrogenase were similar to those of human cytoplasmic E3 isozyme in substrate specificity and kinetic constants for substrates. The primary structure of four tryptic peptides was also similar; only two substitutions, at most, per peptide were observed. Thus, betaine aldehyde dehydrogenase is not a specific enzyme, as formerly believed; activity with betaine aldehyde is a property of aldehyde dehydrogenase (EC 1.2.1.3), which has broad substrate specificity. Up to the present time the enzyme was thought to be cytoplasmic in mammals. This report establishes, for the first time, mitochondrial subcellular localization for aldehyde dehydrogenase, which dehydrogenates betaine aldehyde, and its colocalization with choline dehydrogenase. Betaine aldehyde dehydrogenation is an important function in the metabolism of choline to betaine, a major osmolyte. Betaine is also important in mammalian organisms as a major methyl group donor and nitrogen source. This is the first purification and characterization of mitochondrial betaine aldehyde dehydrogenase from any mammalian species.
    Relation: Biochemistry and Cell Biology 77, pp.179-187
    Appears in Collections:[Graduate Institue of Life Sciences] Journal Article

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