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Smith Smith, Hopkinson Hopkinson, Harris Harris (1973a)
Studies on the subunit structure and molecular size of the human alcohol dehydrogenase isozymes determined by the different loci, adh 1 adh 2 and adh 3ann. hunt. genet., 36
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(1983)
Isoxymen of human liver alcohol dehydrogenase
W. Bosron, Ting-kai Li, L. Lange, W. Dafeldecker, B. Vallée (1977)
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R. Bühler, J. Wartburg (1982)
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Moyra Smith, D. Hopkinson, H. Harris (1972)
Alcohol dehydrogenase isozymes in adult human stomach and liver: evidence for activity of the ADH3 locusAnnals of Human Genetics, 35
D. Strydom, B. Vallée (1982)
Characterization of human alcohol dehydrogenase isoenzymes by high-performance liquid chromatographic peptide mapping.Analytical biochemistry, 123 2
Moyra Smith, D. Hopkinson, H. Harris (1973)
Studies on the subunit structure and molecular size of the human alcohol dehydrogenase isozymes determined by the different loci, ADH1ADH2, and ADH3Annals of Human Genetics, 36
W. Bosron, L. Magnes, T. Li (1983)
Kinetic and electrophoretic properties of native and recombined isoenzymes of human liver alcohol dehydrogenase.Biochemistry, 22 8
F. Wagner, A. Burger, B. Vallée (1983)
Kinetic properties of human liver alcohol dehydrogenase: oxidation of alcohols by class I isoenzymes.Biochemistry, 22 8
Moyra Smith, D. Hopkinson, H. Harris (1973)
Studies on the properties of the human alcohol dehydrogenase isozymes determined by the different loci ADH1, ADH2, ADH3Annals of Human Genetics, 37
B. Roche, E. Azoulay (1969)
Régulation des alcool‐déshydrogénases chez Saccharomyces cerevisiaeFEBS Journal, 8
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A. Adinolfi, M. Adinolfi, D. Hopkinson, H. Harris (1978)
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Roche Roche, Azoulay Azoulay (1969)
régulation des alcool‐déshydrogénases chez saecharomyces cerevisiaeeur. j. biochem., 8
Summary 1. The recently identified χ‐ADH isozyme was purified from human liver and used to raise immune sera. 2. The χ form of ADH showed no structural resemblance to the ADH1, ADH2 and ADH3 (class I) or ADH4 (class II) isozymes, as judged by its immunological properties. 3. χ‐ADH was found in most human tissues including fetal specimens of 16 weeks gestational age and showed a preference for long chain primary alcohols with a double bond in the β position. 4. We conclude that the locus, designated ADH5, encoding the χ isozyme has a separate evolutionary origin from the other ADH genes.
Annals of Human Genetics – Wiley
Published: Jan 1, 1984
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