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Biochemical Genetics

, Volume 20, Issue 3–4, pp 297–313 | Cite as

Synthesis and degradation of alcohol dehydrogenase in wild-type and Adh-null activity mutants of Drosophila melanogaster

  • Joseph G. Pelliccia
  • William Sofer
Article

Abstract

Both the amount and the size of alcohol dehydrogenase-like cross-reacting material was determined in 14 ethyl methanesulfonate (EMS)-induced alcohol dehydrogenase-null activity mutants. In 11 mutants cross-reacting material of the same apparent molecular weight as alcohol dehydrogenase was detected, while in 3 mutants no cross-reacting material was found. In all cases, the amount of cross-reacting material found in the mutants was lower than that in wild-type flies. High, intermediate, and low cross-reacting material-producing mutants showed similar initial rates of incorporation of labeled amino acid into alcohol dehydrogenase-like protein, presumably reflecting similar rates of synthesis. If the rate of synthesis of cross-reacting material is the same in the mutants as in the wild type, then the different levels of cross-reacting material must be due to different rates of degradation.

Key words

alcohol dehydrogenase Adh-null mutants protein synthesis protein degradation 

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Copyright information

© Plenum Publishing Corporation 1982

Authors and Affiliations

  • Joseph G. Pelliccia
    • 1
  • William Sofer
    • 1
  1. 1.Department of BiologyJohns Hopkins UniversityBaltimore

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