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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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Published in: | Biochemical genetics 1980-04, Vol.18 (3-4), p.339-351 |
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container_end_page | 351 |
container_issue | 3-4 |
container_start_page | 339 |
container_title | Biochemical genetics |
container_volume | 18 |
creator | Reddy, A R Pelliccia, J G Sofer, W |
description | 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. |
doi_str_mv | 10.1007/BF00484247 |
format | article |
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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. 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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.</description><subject>Alcohol Oxidoreductases - genetics</subject><subject>Animals</subject><subject>Chromatography, Affinity</subject><subject>Drosophila melanogaster - drug effects</subject><subject>Drosophila melanogaster - enzymology</subject><subject>Drosophila melanogaster - genetics</subject><subject>Ethyl Methanesulfonate - pharmacology</subject><subject>Hydroxyapatites</subject><subject>Mutation</subject><subject>Peptide Fragments - analysis</subject><subject>Precipitin Tests</subject><subject>Trypsin</subject><issn>0006-2928</issn><issn>1573-4927</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1980</creationdate><recordtype>article</recordtype><recordid>eNpFkE1Lw0AQhhdRaq1evAt7FqL7mU281WpVKHjRq2GzM2sj-SLZCvHXm9Kgp5dhnncGHkIuObvhjJnb-zVjKlFCmSMy59rISKXCHJM5YyyORCqSU3LW91_jmDKlZmQWG5Moo-bkYwnbqMZPG4pvpNUu2Dr0dxQwoAtFU9PGU1tTWwbsEGjohjYUjrY4BiAtxtXUolj_DBXuCw9d0zfttijtOTnxtuzxYsoFeV8_vq2eo83r08tquYmcSESIJCTcgXax8eC4S6zgXkhtbe5S60E4UABegwAppYacWc3SHFwujJeap3JBrg933fi679BnbVdUthsyzrK9o-zf0QhfHeB2l1cIf-gkRf4C_D9jIA</recordid><startdate>198004</startdate><enddate>198004</enddate><creator>Reddy, A R</creator><creator>Pelliccia, J G</creator><creator>Sofer, W</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>198004</creationdate><title>Adh-negative mutants: detection of an altered tryptic peptide in a mutant enzyme of Drosophila</title><author>Reddy, A R ; Pelliccia, J G ; Sofer, W</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c282t-3d81cd5c67fdc1c8a21f235aabc9afd2cd4ddf5d2d3335db0a509bdcb27f35193</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1980</creationdate><topic>Alcohol Oxidoreductases - genetics</topic><topic>Animals</topic><topic>Chromatography, Affinity</topic><topic>Drosophila melanogaster - drug effects</topic><topic>Drosophila melanogaster - enzymology</topic><topic>Drosophila melanogaster - genetics</topic><topic>Ethyl Methanesulfonate - pharmacology</topic><topic>Hydroxyapatites</topic><topic>Mutation</topic><topic>Peptide Fragments - analysis</topic><topic>Precipitin Tests</topic><topic>Trypsin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Reddy, A R</creatorcontrib><creatorcontrib>Pelliccia, J G</creatorcontrib><creatorcontrib>Sofer, W</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><jtitle>Biochemical genetics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Reddy, A R</au><au>Pelliccia, J G</au><au>Sofer, W</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Adh-negative mutants: detection of an altered tryptic peptide in a mutant enzyme of Drosophila</atitle><jtitle>Biochemical genetics</jtitle><addtitle>Biochem Genet</addtitle><date>1980-04</date><risdate>1980</risdate><volume>18</volume><issue>3-4</issue><spage>339</spage><epage>351</epage><pages>339-351</pages><issn>0006-2928</issn><eissn>1573-4927</eissn><abstract>Adhnll is an ethyl methanesulfonate induced mutant that lacks detectable alcohol dehydrogenase activity. 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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 |
title | Adh-negative mutants: detection of an altered tryptic peptide in a mutant enzyme of Drosophila |
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