Adh-negative mutants: detection of an altered tryptic peptide in a mutant enzyme of Drosophila

Adhnll is an ethyl methanesulfonate induced mutant that lacks detectable alcohol dehydrogenase activity. A number of indirect lines of evidence have indicated that the mutation responsible for this loss in enzyme activity is localized in the Adh structural gene. We present more direct evidence for t...

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Bibliographic Details
Published in:Biochemical genetics 1980-04, Vol.18 (3-4), p.339-351
Main Authors: Reddy, A R, Pelliccia, J G, Sofer, W
Format: Article
Language:English
Subjects:
Alcohol Oxidoreductases - genetics
Animals
Chromatography, Affinity
Drosophila melanogaster - drug effects
Drosophila melanogaster - enzymology
Drosophila melanogaster - genetics
Ethyl Methanesulfonate - pharmacology
Hydroxyapatites
Mutation
Peptide Fragments - analysis
Precipitin Tests
Trypsin
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Summary:Adhnll is an ethyl methanesulfonate induced mutant that lacks detectable alcohol dehydrogenase activity. A number of indirect lines of evidence have indicated that the mutation responsible for this loss in enzyme activity is localized in the Adh structural gene. We present more direct evidence for this hypothesis here. Utilizing a newly developed procedure for comparing tryptic peptides of Drosophila alcohol dehydrogenase obtained from different strains, we show that the alcohol dehydrogenase-like protein isolated from Adhnll exhibits an altered peptide profile when compared to that of wild type. The implications of this finding as well as the utility of the method for attacking other genetic and developmental problems are discussed.
ISSN:0006-2928
1573-4927
DOI:10.1007/BF00484247