Storage protein mobilization during germination and early seedling growth of Zea mays
Identifieur interne : 000959 ( Istex/Corpus ); précédent : 000958; suivant : 000960Storage protein mobilization during germination and early seedling growth of Zea mays
Auteurs : Pamela Camp Hay ; Tina Ramsaur ; Carlene Smith ; Jan A. MiernykSource :
- Physiologia Plantarum [ 0031-9317 ] ; 1991-03.
English descriptors
- KwdEn :
Abstract
Changes in general protease activity and the levels of the zein storage proteins were monitored during germination and early seedling growth of maize (Zea mays L. inbred A636). General endosperm endoprotease activity, measured in vitro using azocasein as a substrate, increased continuously to day 5 and remained high thereafter. The increase was in parallel with the loss of zein protein as determined by immunoblot analysis, with a total loss of detectable zein by 10 days after inhibition of the seeds. A method was developed for the specific in vitro assay of zein degrading activity by monitoring the release of soluble radioactivity from the immobilized storage protein. The in vitro pH optimum for both general protease and zein degrading activities in homogenates prepared from isolated endosperm was 4.0. However, the curve for general protease activity was asymmetrical suggesting the presence of more than 1 protease. This was verified by activity staining of gelatin‐containing polyacrylamide gels, which suggested the presence of 3 major and 3 minor protease activities. Both general protease and zein‐specific activities were enhanced more than 2‐fold when 2‐mercaptoethanol (ME) was included in the assays, and both were inhibited by fhiol‐protease directed compounds. Most of the general protease activity but none of the zein‐specific protease activity bound to con A‐Sepharose. Both the con A‐binding and nonbinding fractions were analyzed using gelatin activity gels. The 3 minor activity bands were present in the fraction which was specifically eluted from the con A column by a‐methyl‐mannoside, while the 3 major activity bands, corresponding to the zein‐specific protease activity, did not bind to the immobilized lectin.
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DOI: 10.1111/j.1399-3054.1991.tb08746.x
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ISTEX:CBFB4478644FDED687513E2DB13452131C231B1CLe document en format XML
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General endosperm endoprotease activity, measured in vitro using azocasein as a substrate, increased continuously to day 5 and remained high thereafter. The increase was in parallel with the loss of zein protein as determined by immunoblot analysis, with a total loss of detectable zein by 10 days after inhibition of the seeds. A method was developed for the specific in vitro assay of zein degrading activity by monitoring the release of soluble radioactivity from the immobilized storage protein. The in vitro pH optimum for both general protease and zein degrading activities in homogenates prepared from isolated endosperm was 4.0. However, the curve for general protease activity was asymmetrical suggesting the presence of more than 1 protease. This was verified by activity staining of gelatin‐containing polyacrylamide gels, which suggested the presence of 3 major and 3 minor protease activities. Both general protease and zein‐specific activities were enhanced more than 2‐fold when 2‐mercaptoethanol (ME) was included in the assays, and both were inhibited by fhiol‐protease directed compounds. Most of the general protease activity but none of the zein‐specific protease activity bound to con A‐Sepharose. Both the con A‐binding and nonbinding fractions were analyzed using gelatin activity gels. The 3 minor activity bands were present in the fraction which was specifically eluted from the con A column by a‐methyl‐mannoside, while the 3 major activity bands, corresponding to the zein‐specific protease activity, did not bind to the immobilized lectin.</div></front></TEI><istex><corpusName>wiley</corpusName><author><json:item><name>Pamela Camp Hay</name><affiliations><json:string>Dept of Biology, Davidson College, Davidson, NC 28036, USA</json:string></affiliations></json:item><json:item><name>Tina Ramsaur</name><affiliations><json:string>Dept of Biology, Davidson College, Davidson, NC 28036, USA</json:string></affiliations></json:item><json:item><name>Carlene Smith</name><affiliations><json:string>Dept of Biology, Davidson College, Davidson, NC 28036, USA</json:string></affiliations></json:item><json:item><name>Jan A. Miernyk</name><affiliations><json:string>Seed Biosynthesis Research Unit, USDA, ARS, Northern Regional Research Center, Peoria. 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General endosperm endoprotease activity, measured in vitro using azocasein as a substrate, increased continuously to day 5 and remained high thereafter. The increase was in parallel with the loss of zein protein as determined by immunoblot analysis, with a total loss of detectable zein by 10 days after inhibition of the seeds. A method was developed for the specific in vitro assay of zein degrading activity by monitoring the release of soluble radioactivity from the immobilized storage protein. The in vitro pH optimum for both general protease and zein degrading activities in homogenates prepared from isolated endosperm was 4.0. However, the curve for general protease activity was asymmetrical suggesting the presence of more than 1 protease. This was verified by activity staining of gelatin‐containing polyacrylamide gels, which suggested the presence of 3 major and 3 minor protease activities. Both general protease and zein‐specific activities were enhanced more than 2‐fold when 2‐mercaptoethanol (ME) was included in the assays, and both were inhibited by fhiol‐protease directed compounds. Most of the general protease activity but none of the zein‐specific protease activity bound to con A‐Sepharose. Both the con A‐binding and nonbinding fractions were analyzed using gelatin activity gels. 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Both general protease and zein‐specific activities were enhanced more than 2‐fold when 2‐mercaptoethanol (ME) was included in the assays, and both were inhibited by fhiol‐protease directed compounds. Most of the general protease activity but none of the zein‐specific protease activity bound to con A‐Sepharose. Both the con A‐binding and nonbinding fractions were analyzed using gelatin activity gels. 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IL 61604, USA.</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en"><keyword xml:id="k1">Endosperm</keyword><keyword xml:id="k2">maize</keyword><keyword xml:id="k3">prolamin</keyword><keyword xml:id="k4">protease</keyword><keyword xml:id="k5">seed germination</keyword><keyword xml:id="k6">storage protein</keyword><keyword xml:id="k7">Zea mays</keyword><keyword xml:id="k8">zein</keyword></keywordGroup><abstractGroup><abstract type="main" xml:lang="en"><p>Changes in general protease activity and the levels of the zein storage proteins were monitored during germination and early seedling growth of maize (<i>Zea mays L</i>. inbred A636). General endosperm endoprotease activity, measured in vitro using azocasein as a substrate, increased continuously to day 5 and remained high thereafter. The increase was in parallel with the loss of zein protein as determined by immunoblot analysis, with a total loss of detectable zein by 10 days after inhibition of the seeds. A method was developed for the specific in vitro assay of zein degrading activity by monitoring the release of soluble radioactivity from the immobilized storage protein. The in vitro pH optimum for both general protease and zein degrading activities in homogenates prepared from isolated endosperm was 4.0. However, the curve for general protease activity was asymmetrical suggesting the presence of more than 1 protease. This was verified by activity staining of gelatin‐containing polyacrylamide gels, which suggested the presence of 3 major and 3 minor protease activities. Both general protease and zein‐specific activities were enhanced more than 2‐fold when 2‐mercaptoethanol (ME) was included in the assays, and both were inhibited by fhiol‐protease directed compounds. Most of the general protease activity but none of the zein‐specific protease activity bound to con A‐Sepharose. Both the con A‐binding and nonbinding fractions were analyzed using gelatin activity gels. The 3 minor activity bands were present in the fraction which was specifically eluted from the con A column by a‐methyl‐mannoside, while the 3 major activity bands, corresponding to the zein‐specific protease activity, did not bind to the immobilized lectin.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Storage protein mobilization during germination and early seedling growth of Zea mays</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Storage protein mobilization during germination and early seedling growth of</title></titleInfo><name type="personal"><namePart type="given">Pamela Camp</namePart><namePart type="family">Hay</namePart><affiliation>Dept of Biology, Davidson College, Davidson, NC 28036, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Tina</namePart><namePart type="family">Ramsaur</namePart><affiliation>Dept of Biology, Davidson College, Davidson, NC 28036, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Carlene</namePart><namePart type="family">Smith</namePart><affiliation>Dept of Biology, Davidson College, Davidson, NC 28036, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Jan A.</namePart><namePart type="family">Miernyk</namePart><affiliation>Seed Biosynthesis Research Unit, USDA, ARS, Northern Regional Research Center, Peoria. 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Miernyk (corresponding author)</description><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article"></genre><originInfo><publisher>Blackwell Publishing Ltd</publisher><place><placeTerm type="text">Oxford, UK</placeTerm></place><dateIssued encoding="w3cdtf">1991-03</dateIssued><edition>Received 13 July, 1990; revised 26 November, 1990</edition><copyrightDate encoding="w3cdtf">1991</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType><extent unit="references">27</extent></physicalDescription><abstract lang="en">Changes in general protease activity and the levels of the zein storage proteins were monitored during germination and early seedling growth of maize (Zea mays L. inbred A636). General endosperm endoprotease activity, measured in vitro using azocasein as a substrate, increased continuously to day 5 and remained high thereafter. The increase was in parallel with the loss of zein protein as determined by immunoblot analysis, with a total loss of detectable zein by 10 days after inhibition of the seeds. A method was developed for the specific in vitro assay of zein degrading activity by monitoring the release of soluble radioactivity from the immobilized storage protein. The in vitro pH optimum for both general protease and zein degrading activities in homogenates prepared from isolated endosperm was 4.0. However, the curve for general protease activity was asymmetrical suggesting the presence of more than 1 protease. This was verified by activity staining of gelatin‐containing polyacrylamide gels, which suggested the presence of 3 major and 3 minor protease activities. Both general protease and zein‐specific activities were enhanced more than 2‐fold when 2‐mercaptoethanol (ME) was included in the assays, and both were inhibited by fhiol‐protease directed compounds. Most of the general protease activity but none of the zein‐specific protease activity bound to con A‐Sepharose. Both the con A‐binding and nonbinding fractions were analyzed using gelatin activity gels. The 3 minor activity bands were present in the fraction which was specifically eluted from the con A column by a‐methyl‐mannoside, while the 3 major activity bands, corresponding to the zein‐specific protease activity, did not bind to the immobilized lectin.</abstract><subject lang="en"><genre>Keywords</genre><topic>Endosperm</topic><topic>maize</topic><topic>prolamin</topic><topic>protease</topic><topic>seed germination</topic><topic>storage protein</topic><topic>Zea mays</topic><topic>zein</topic></subject><relatedItem type="host"><titleInfo><title>Physiologia Plantarum</title></titleInfo><genre type="Journal">journal</genre><identifier type="ISSN">0031-9317</identifier><identifier type="eISSN">1399-3054</identifier><identifier type="DOI">10.1111/(ISSN)1399-3054</identifier><identifier type="PublisherID">PPL</identifier><part><date>1991</date><detail type="volume"><caption>vol.</caption><number>81</number></detail><detail type="issue"><caption>no.</caption><number>3</number></detail><extent unit="pages"><start>377</start><end>384</end><total>8</total></extent></part></relatedItem><identifier type="istex">CBFB4478644FDED687513E2DB13452131C231B1C</identifier><identifier type="DOI">10.1111/j.1399-3054.1991.tb08746.x</identifier><identifier type="ArticleID">PPL377</identifier><recordInfo><recordContentSource>WILEY</recordContentSource><recordOrigin>Blackwell Publishing Ltd</recordOrigin></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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|clé= ISTEX:CBFB4478644FDED687513E2DB13452131C231B1C
|texte= Storage protein mobilization during germination and early seedling growth of Zea mays
}}
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