Adh-negative mutants: Detection of an altered tryptic peptide in a mutant enzyme of Drosophila |
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Authors: | A. R. Reddy Joseph G. Pelliccia William Sofer |
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Affiliation: | (1) Department of Biology, Johns Hopkins University, 21218 Baltimore, Maryland;(2) Present address: School of Life Sciences, Central University of Hyderabad, 500001 (A.P.) Hyderabad, India;(3) Present address: Department of Biology, Bates College, 04240 Lewiston, Maine |
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Abstract: | 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 locoalized 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.This work was supported by grants from the NIH (GM-18254 and ES-01527) and by a contract from the Department of Energy (EY-76-S-02-2965).Contribution No. 1050 from the Department of Biology, John Hopkins University, Baltimore, Maryland 21218. |
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Keywords: | alcohol dehydrogenase Adh-negative mutants Adh-tryptic peptides |
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