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Human erythrocyte aldehyde dehydrogenase (aldehyde:NAD+ oxidoreductase, EC 1.2.1.3) was purified to apparent homogeneity. The native enzyme has a molecular weight of about 210,000 as determined by gel filtration, and SDS-polyacrylamide gel electrophoresis of this enzyme yields a single protein and with a molecular weight of 51,500, suggesting that the native enzyme may be a tetramer. The enzyme has a relatively low Km for NAD (15 microM) and a high sensitivity to disulfiram. Disulfiram inhibits the enzyme activity rapidly and this inhibition is apparently of a non-competitive nature. In kinetic characteristic and sensitivity to disulfiram, erythrocyte aldehyde dehydrogenase closely resembles the cytosolic aldehyde dehydrogenase found in the liver of various species of mammalians.
K Inoue, and
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K Yamasawa
January 1990,
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K Inoue, and
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K Inoue, and
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K Inoue, and
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K Inoue, and
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K Inoue, and
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K Yamasawa
January 1982,
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K Inoue, and
H Nishimukai, and
K Yamasawa
April 1988,
Archives of biochemistry and biophysics,
K Inoue, and
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K Yamasawa
July 1962,
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K Inoue, and
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K Yamasawa
April 1997,
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