Loading…

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...

Full description

Saved in:
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:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c282t-3d81cd5c67fdc1c8a21f235aabc9afd2cd4ddf5d2d3335db0a509bdcb27f35193
cites cdi_FETCH-LOGICAL-c282t-3d81cd5c67fdc1c8a21f235aabc9afd2cd4ddf5d2d3335db0a509bdcb27f35193
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
fullrecord <record><control><sourceid>pubmed_cross</sourceid><recordid>TN_cdi_crossref_primary_10_1007_BF00484247</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>6778474</sourcerecordid><originalsourceid>FETCH-LOGICAL-c282t-3d81cd5c67fdc1c8a21f235aabc9afd2cd4ddf5d2d3335db0a509bdcb27f35193</originalsourceid><addsrcrecordid>eNpFkE1Lw0AQhhdRaq1evAt7FqL7mU281WpVKHjRq2GzM2sj-SLZCvHXm9Kgp5dhnncGHkIuObvhjJnb-zVjKlFCmSMy59rISKXCHJM5YyyORCqSU3LW91_jmDKlZmQWG5Moo-bkYwnbqMZPG4pvpNUu2Dr0dxQwoAtFU9PGU1tTWwbsEGjohjYUjrY4BiAtxtXUolj_DBXuCw9d0zfttijtOTnxtuzxYsoFeV8_vq2eo83r08tquYmcSESIJCTcgXax8eC4S6zgXkhtbe5S60E4UABegwAppYacWc3SHFwujJeap3JBrg933fi679BnbVdUthsyzrK9o-zf0QhfHeB2l1cIf-gkRf4C_D9jIA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Adh-negative mutants: detection of an altered tryptic peptide in a mutant enzyme of Drosophila</title><source>SpringerLink_过刊(NSTL购买)</source><creator>Reddy, A R ; Pelliccia, J G ; Sofer, W</creator><creatorcontrib>Reddy, A R ; Pelliccia, J G ; Sofer, W</creatorcontrib><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.</description><identifier>ISSN: 0006-2928</identifier><identifier>EISSN: 1573-4927</identifier><identifier>DOI: 10.1007/BF00484247</identifier><identifier>PMID: 6778474</identifier><language>eng</language><publisher>United States</publisher><subject>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</subject><ispartof>Biochemical genetics, 1980-04, Vol.18 (3-4), p.339-351</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c282t-3d81cd5c67fdc1c8a21f235aabc9afd2cd4ddf5d2d3335db0a509bdcb27f35193</citedby><cites>FETCH-LOGICAL-c282t-3d81cd5c67fdc1c8a21f235aabc9afd2cd4ddf5d2d3335db0a509bdcb27f35193</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6778474$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Reddy, A R</creatorcontrib><creatorcontrib>Pelliccia, J G</creatorcontrib><creatorcontrib>Sofer, W</creatorcontrib><title>Adh-negative mutants: detection of an altered tryptic peptide in a mutant enzyme of Drosophila</title><title>Biochemical genetics</title><addtitle>Biochem Genet</addtitle><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.</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. 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.</abstract><cop>United States</cop><pmid>6778474</pmid><doi>10.1007/BF00484247</doi><tpages>13</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0006-2928
ispartof Biochemical genetics, 1980-04, Vol.18 (3-4), p.339-351
issn 0006-2928
1573-4927
language eng
recordid cdi_crossref_primary_10_1007_BF00484247
source SpringerLink_过刊(NSTL购买)
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
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-07T10%3A15%3A38IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-pubmed_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Adh-negative%20mutants:%20detection%20of%20an%20altered%20tryptic%20peptide%20in%20a%20mutant%20enzyme%20of%20Drosophila&rft.jtitle=Biochemical%20genetics&rft.au=Reddy,%20A%20R&rft.date=1980-04&rft.volume=18&rft.issue=3-4&rft.spage=339&rft.epage=351&rft.pages=339-351&rft.issn=0006-2928&rft.eissn=1573-4927&rft_id=info:doi/10.1007/BF00484247&rft_dat=%3Cpubmed_cross%3E6778474%3C/pubmed_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c282t-3d81cd5c67fdc1c8a21f235aabc9afd2cd4ddf5d2d3335db0a509bdcb27f35193%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_id=info:pmid/6778474&rfr_iscdi=true