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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
Article

Abstract

Alcohol dehydrogenase (ADH; EC 1.1.1.1) 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 

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Copyright information

© Plenum Publishing Corporation 1983

Authors and Affiliations

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

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