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    Please use this identifier to cite or link to this item: http://tkuir.lib.tku.edu.tw:8080/dspace/handle/987654321/61844


    Title: Betaine aldehyde dehydrogenase from rat liver mitochondrial matrix
    Authors: Pietruszko, Regina;Chern, Ming-kai
    Contributors: 淡江大學生命科學研究所
    Keywords: Betaine aldehyde dehydrogenase;Mitochondria;Rat liver;Localization
    Date: 2001-01
    Issue Date: 2013-05-31 11:33:20 (UTC+8)
    Publisher: Shannon: Elsevier Ireland Ltd
    Abstract: An NAD-linked aldehyde dehydrogenase which in addition to aliphatic and aromatic aldehydes, metabolizes aminoaldehydes and betaine aldehyde, has been purified to homogeneity from male Sprague–Dawley rat liver mitochondria. The properties of the rat mitochondrial enzyme are similar to those of a rat liver cytoplasmic betaine aldehyde dehydrognase and the human cytoplasmic E3 isozyme. The primary structure. of four tryptic peptides were also similar; only one difference in primary structure was observed. The close similarity of properties of the cytoplasmic with the mitochondrial form suggest that the cytoplasmic and mitochondrial betaine aldehyde dehydrogenase may be coded for by the same nuclear gene. Investigation of the mitochondrial form by isoelectric focusing resulted in visualization of multiple forms, different from those seen in the cytoplasm suggesting that the enzyme may be processed in the mitochondria.
    Relation: Chemico-Biological Interactions 130-132, pp.193-199
    DOI: 10.1016/S0009-2797(00)00277-5
    Appears in Collections:[生命科學研究所] 期刊論文

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