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XB-ART-30070
Biochem Genet 1983 Oct 01;219-10:1003-17. doi: 10.1007/bf00483956.
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Alcohol dehydrogenase isozymes in the clawed frog, Xenopus laevis.

Wesolowski MH , Lyerla TA .


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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 10 mM 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.

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Species referenced: Xenopus laevis
Genes referenced: adh1 adh1a adh1b adh1c

References [+] :
Etkin, Regulation of lactate dehydrogenase (LDH) and alcohol dehydrogenase (ADH) synthesis in liver nuclei, following their transfer into oocytes. 1976, Pubmed