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    Please use this identifier to cite or link to this item: http://tkuir.lib.tku.edu.tw:8080/dspace/handle/987654321/61855

    Title: Human aldehyde dehydrogenase E3 isozyme is a betaine aldehyde dehydrogenase
    Authors: Chern, Ming-kai;Pietruszko, Regina
    Contributors: 淡江大學生命科學研究所
    Date: 1995-08
    Issue Date: 2013-05-31 11:33:25 (UTC+8)
    Publisher: Maryland Heights: Academic Press
    Abstract: The E3 isozyme of human aldehyde dehydrogenase (EC, with broad substrate specificity, which also catalyzes dehydrogenation of 4-aminobutyraldehyde, was purified and sequenced recently (1,3). It has been shown during this investigation to have betaine aldehyde dehydrogenase activity. Betaine aldehyde and 4-aminobutyraldehyde activities copurified on six chromatographic columns. Molecular properties of the homogeneous product were identical with those of E3 isozyme. Activity with betaine aldehyde was considerably higher than that with 4-aminobutyraldehyde, the best known substrate. Thus, human E3 isozyme and betaine aldehyde dehydrogenase (EC are the same enzyme.
    Relation: Biochemical and Biophysical Research Communications 213(2), pp.561-568
    DOI: 10.1006/bbrc.1995.2168
    Appears in Collections:[生命科學研究所] 期刊論文

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