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Further studies on the alcohol dehydrogenases in barley: evidence for a third alcohol dehydrogenase locus and data on the effect of an alcohol dehydrogenase1 null mutation in homozygous and in heterozygous condition

Published online by Cambridge University Press:  14 April 2009

N. P. Harberd
Affiliation:
Department of Genetics, University of Cambridge, Downing Street, Cambridge CB2 3EH
K. J. R. Edwards
Affiliation:
Department of Genetics, University of Cambridge, Downing Street, Cambridge CB2 3EH
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Summary

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This paper presents evidence that the alcohol dehydrogenases (ADHs) in barley are specified by three loci. Six distinct ADH isozymes are observed following native slab polyacrylamide gel electrophoresis of crude extracts from flooded wild-type roots. Three of these isozymes are missing in flooded roots of plants homozygous for the Adhl-M9 mutation. The results also indicate that a simple binomial model (incorporating random dimerization and no inhibitive interaction of the two subunit species within heterodimers) is unable to account for the distribution of the total ADH activity between the ADH isozymes observed. Finally, the level and distribution of ADH activity in heterozygous (Adhl+ / Adhl-M9) flooded roots is not what would be expected if these contain only one-half of the available ADH1 protomers and the same frequency of available ADH2 and ADH3 protomers as is contained in the flooded roots of wild-type homozygotes (Adhl + / Adhl + ).

Type
Research Article
Copyright
Copyright © Cambridge University Press 1983

References

REFERENCES

Banuett-Bourrillon, F. & Hague, D. K. (1979). Genetic analysis of the alcohol dehydrogenase isozymes in Pearl Millet (Pennisetum typhoides). Biochemical Genetics 17, 537552.CrossRefGoogle ScholarPubMed
Briggs, D. E. (1978). Barley. London: Chapman and Hall.CrossRefGoogle Scholar
Brown, A. H. D. (1980). Genetic basis of the alcohol dehydrogenase polymorphism in Hordeum spontaneum. Journal of Heredity 70, 127128.CrossRefGoogle Scholar
Fischer, M. & Schwartz, D. (1973). Dissociation and reassociation of maize ADH: Allelic differences in requirement for zinc. Molecular and General Genetics 127, 3338.CrossRefGoogle Scholar
Freeling, M. (1973). Simultaneous induction by anaerobiosis or 2,4-D of multiple enzymes specified by two unlinked genes: Differential Adh1-Adh2 expression in maize. Molecular and General Genetics 127, 215227.CrossRefGoogle ScholarPubMed
Harberd, N. P. (1981). A genetical investigation of the alcohol dehydrogenase system in barley. Ph.D. dissertation, University of Cambridge.Google Scholar
Harberd, N. P. & Edwards, K. J. R. (1982). A mutational analysis of the alcohol dehydrogenase system in barley. Heredity 48, 187195.CrossRefGoogle Scholar
Hart, G. E. (1971). Alcohol dehydrogenase isozymes of Trtitcum: dissociation and recombination of subunits. Molecular and General Genetics 111, 6165.CrossRefGoogle Scholar
Ohno, S. (1970). Evolution by Gene Duplication. New York: Springer.CrossRefGoogle Scholar
Sedmak, J. J. & Grossberg, S. E. (1977). A rapid, sensitive and versatile assay for protein using Coomasie Blue G250. Analytical Biochemistry 79, 544552.CrossRefGoogle Scholar
Steel, R. G. D. & Torrie, J. H. (1960). Principles and Procedures of Statistics. New York: McGraw-Hill.Google Scholar
Zuckerkandl, E. (1978). Multilocus enzymes, gene regulation and genetic sufficiency. Journal of Molecular Evolution 12, 5789.CrossRefGoogle ScholarPubMed