Biochemical Genetics

, Volume 21, Issue 9–10, pp 1003–1017 | Cite as

Alcohol dehydrogenase isozymes in the clawed frog, Xenopus laevis

  • Mary H. Wesolowski
  • Timothy A. Lyerla


Alcohol dehydrogenase (ADH; EC activity in Xenopus laevis was highest in liver tissue, with decreasing activities in kidney, heart, and gut tissues, respectively. Essentially no activity was found among other tissues screened, including lung, ovary, eye, and testes. Also, there was no apparent sexual dimorphism of ADH activity in either liver or kidney tissue. All ADH isozymes were inhibited by 10mm pyrazole, and no eye-specific retinol dehydrogenase activity was detected on starch gel electropherograms. Isozyme patterns from 418 offspring from 11 different crosses could be explained genetically assuming the presence of two structural genes coding for ADH production: one carrying two electrophoretically separable variants and the other showing quantitative variation in its expression. The ADH system in X. laevis should be useful for studies concerning the molecular mechanisms governing the expression of ADH activity in vertebrate development.

Key words

Xenopus laevis alcohol dehydrogenase isozymes tissue specificity genetic basis 


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Brändén, C. I., Jornvall, H., Eklund, H., and Furugren, B. (1975). Alcohol dehydrogenase. In Boyer, P. D. (ed.), The Enzymes, Vol. 11. Oxidation-Reduction, Part A 3rd ed., Academic Press, New York, pp. 104–190.Google Scholar
  2. Etkin, L. D. (1976). Regulation of lactate dehydrogenase (LDH) and alcohol dehydrogenase (ADH) synthesis in liver nuclei, following their transfer into oocytes. Dev. Biol. 52201.Google Scholar
  3. Etkin, L. D. (1982). Analysis of the mechanisms involved in gene regulation and cell differentiation by microinjection of purified genes and somatic cell nuclei into amphibian oocytes and eggs. Differentiation 21149.Google Scholar
  4. Frankel, J. S. (1980). Expression of alcohol dehydrogenase during pearl danio development. J. Hered. 71430.Google Scholar
  5. Goedde, H. W., Agarwal, D. P., and Harada, S., (1980), Genetic studies on alcohol-metabolizing enzymes: Detection of isozymes in human hair roots. Enzyme 25281.Google Scholar
  6. Gurdon, J. B. (1967). African clawed frogs. In Wilt, F. H., and Wessells, N. K. (eds.), Methods in Developmental Biology Thomas Y. Crowell, New York, pp. 75–84.Google Scholar
  7. Hitzeroth, H., Klose, J., Ohno, S., and Wolf, U. (1968). Asynchronous activation of parental alleles at the tissue-specific gene loci observed in hybrid trout during early development. Biochem. Genet. 11287.Google Scholar
  8. Koen, A. L., and Shaw, C. R. (1966). Retinol and alcohol dehydrogenase in retina and liver. Biochim. Biophys. Acta 12848.Google Scholar
  9. Le Vine, J. P., and Hadley, L. R. (1975). Gene activation of alcohol dehydrogenase in Japanese quail and chicken-quail hybrid embryos. Biochem. Genet. 13435.Google Scholar
  10. Li, T. K., Bosron, W. F., Dafeldecker, W. P., Lange, L. G., and Vallee, B. L. (1977). Isolation of π-alcohol dehydrogenase of human liver: Is it a determinant of alcoholism? Proc. Natl. Acad. Sci. 744378.Google Scholar
  11. Nieuwkoop, P. D., and Faber, J. (1967). Normal Table of Xenopus laevis (Daudin) North-Holland, Amsterdam.Google Scholar
  12. Ohno, S., Stenius, C., and Christian L. C., (1970). Sex difference in alcohol metabolism, androgenic steroid as an inducer of kidney alcohol dehydrogenase. Clin. Genet. 135.Google Scholar
  13. Pietruszko, R., Crawford, K., and Lester, D. (1973). Comparison of substrate specificity of alcohol dehydrogenase from human liver, horse liver, and yeast towards saturated and 2-enoic alcohols and aldehydes. Arch. Biochem. Biophys. 15950.Google Scholar
  14. Räihä, N. C. R., Koskinen, M., and Pikkarainen, P. (1967). Developmental changes in alcohol-dehydrogenase activity in rat and guinea-pig liver. Biochem. J. 103623.Google Scholar
  15. Rossman, A. G., Liljas, A., Bräandén, C.-I., and Banaszak, L. J. (1975). Evolutionary and structural relationships among dehydrogenases. In Boyer, P. D. (ed.), The Enzymes, Vol. 11 3rd ed., Academic Press, New York, pp. 61–102.Google Scholar
  16. Sedmak, J. J., and Grossberg, S. E. (1977). A rapid, sensitive, and versatile assay for protein using Coomassie brilliant blue G250. Anal. Biochem. 79544.Google Scholar
  17. Theorell, H., Taniguchi, S., Åkeson, Å., and Skursky, L. (1966). Crystallization of a separate steroid-active liver alcohol dehydrogenase. Biochem. Biophys. Res. Comm. 24603.Google Scholar
  18. Wesolowski, M. H. (1978). The Developmental Appearance of Tissue-Specific “Luxury” Enzymes in Xenopus laevis: Gut Hexokinase and Liver Alcohol Dehydrogenase M. A. thesis, Clark University, Worcester, Mass.Google Scholar
  19. Wesolowski, M. H., and Lyerla, T. A. (1979). The developmental appearance of hexokinase and alcohol dehydrogenase in Xenopus laevis. J. Exp. Zool. 210211.Google Scholar
  20. Wolf, D. P., and Hedrick, H. L. (1971). A molecular approach to fertilization. II. Viability and artificial fertilization of Xenopus laevis. Dev. Biol. 25348.Google Scholar

Copyright information

© Plenum Publishing Corporation 1983

Authors and Affiliations

  • Mary H. Wesolowski
    • 1
  • Timothy A. Lyerla
    • 1
  1. 1.Department of BiologyClark UniversityWorcester

Personalised recommendations