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- W2026997521 abstract "Human alcohol dehydrogenase in crude liver extracts separates on starch gels at pH 8.5 into seven bands. The four fastest-migrating bands were purified and separated into component isoenzymes by chromatography on carboxymethyl cellulose. Six distinct isoenzymes were separated. 1A, 1B, 2, 3A, 3B, and 4; the number denotes band position on starch gel and the letters distinct subunit composition. Two distinct isoenzymes have been shown to occupy band 1 on starch gels and two distinct enzymes occupy band 3. Bands 2 and 4 are also suspected to be heterogeneous. The differences among isoenzymes were established by dissociation and reconstitution, electrophoresis, kinetics, and fluorometry. Isoenzymes 1A and 1B are distinguishable from each other by fluorometry and kinetics but appear to be identical on electrophoresis before and after dissociation and reconstitution. Isoenzymes 3A and 3B are distinguishable by electrophoresis at pH 7.0 and also form different products after dissociation and reconstitution. While isoenzyme 3A appears to be related structurally to the isoenzyme(s) occupying band 2 on starch gels at pH 8.5, isoenzyme 3B is related to the isoenzyme(s) occupying position 1. All of the isolated isoenzymes have low activity with ethanol; the most active has about 30% of the activity of horse liver isoenzyme EE." @default.
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- W2026997521 date "1972-11-01" @default.
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- W2026997521 title "Heterogeneity of alcohol dehydrogenase from human liver" @default.
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- W2026997521 doi "https://doi.org/10.1016/0003-9861(72)90446-8" @default.
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