Abstract
LIVER alcohol dehydrogenase (ADH; EC 1.1.1.1) exists in multiple molecular forms—isoenzymes—in many species1–3. Von Wartburg et al.4 and Blair and Vallee5 have purified ADH from human liver and found three chromatographically distinct active forms of the enzyme. Many of the catalytic properties of the human enzyme resemble those of the enzyme from animal liver although differences in the Michael is constants for substrates and coenzyme have been found.
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References
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PIKKARAINEN, P., RÄIHÄ, N. Change in Alcohol Dehydrogenase Isoenzyme Pattern during Development of Human Liver. Nature 222, 563–564 (1969). https://doi.org/10.1038/222563a0
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DOI: https://doi.org/10.1038/222563a0
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