Abstract
Horse liver contains previously unrecognized isozymes of alcohol dehydrogenase. In contrast to the molecular forms identified up to now, under the conditions employed these variants migrate toward the anode on starch gel electrophoresis and were separated from the cathodic isozymes by DEAE-cellulose chromatography. They were then purified on agarose-hexane-AMP. Their physicochemical and compositional characteristics are similar to those x alcohol dehydrogenases from human liver. Like these and similar ones from simian liver, they retain most of their activity in the presence of10 mm 4-methylpyrazole, oxidize short-chain primary alcohols very poorly, and appear to prefer longer chain primary alcohols and ω-hydroxy fatty acids as substrates.
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Dafeldecker, W.P., Vallee, B.L. χ alcohol dehydrogenase isozymes of horse liver. J Protein Chem 1, 59–69 (1982). https://doi.org/10.1007/BF01025551
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DOI: https://doi.org/10.1007/BF01025551