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Plant Physiology 65:518-522 (1980)
© 1980 American Society of Plant Biologists

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Articles

Wheat Alcohol Dehydrogenase Isozymes

PURIFICATION, CHARACTERIZATION, AND GENE EXPRESSION 1

Pat J. Langston2, C. Nick Pace and Gary E. Hart

Department of Biochemistry and Biophysics, Texas A&M University and Texas Agricultural Experiment Station, College Station, Texas 77843, Department of Plant Sciences, Texas A&M University and Texas Agricultural Experiment Station, College Station, Texas 77843

Evidence in support of the hypothesis of gene expression and subunit association suggested earlier for Triticum alcohol dehydrogenase has been obtained through purification and partial characterization of the enzyme from tetraploid wheat. Three isozymes of alcohol dehydrogenase were separated and purified to apparent homogeneity using streptomycin sulfate precipitation, gel filtration chromatography, and anion exchange chromatography. The isozymes are dimers with the same molecular weight (116,000 ± 2,000), but significantly different isoelectric pH values. The Michaelis constants for NAD+ and ethanol are 0.1 millimolar and 12 millimolar, respectively. The substrate specificity of the three alcohol dehydrogenase isozymes was investigated.

2 Send reprint requests to: P. J. Langston, Biochemistry Department, University of Minnesota, St. Paul, Minn. 55108.

1 The investigations reported were included in the dissertation submitted by P. J. L. to the Graduate College, Texas A&M University, in partial fulfillment of the requirements for the Ph.D. degree. This paper is Technical Article No. 15481 of the Texas Agricultural Experiment Station.






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