Jerusalem artichoke invertases—Immunocharacterization of a soluble form and its putative precursor
Identifieur interne : 000B49 ( Istex/Corpus ); précédent : 000B48; suivant : 000B50Jerusalem artichoke invertases—Immunocharacterization of a soluble form and its putative precursor
Auteurs : P. Goupil ; Y. Croisille ; F. Croisille ; G. LedoigtSource :
- Plant Science [ 0168-9452 ] ; 1988.
Abstract
Using AcA 22 Ultrogel immobilized anti-yeast invertase antibodies a soluble acid invertase (β D fructofuranoside fructohydrolase, EC 3.2.1.26), representing only part of the total acid invertase activity, has been purified from Helianthus tuberosus shoot extracts. Under denaturing conditions (SDS-PAGE) this enzyme usually yields a 58 kDa polypeptide. From one particular extract out of nine, however, a second acid invertase form, yielding essentially a 30 kDa polypeptide, was obtained. Furthermore, after in vitro translation of either polysomal RNA followed by immunoprecipitation, or mRNA isolated from previously immunoselected polysomes, a 97 kDa polypeptide which could be the precursor of both acid invertase forms was observed. The possible physiological significance of these observations is discussed.
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DOI: 10.1016/0168-9452(88)90054-4
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Ledoigt</name><affiliation><mods:affiliation>To whom correspondence should be sent.</mods:affiliation></affiliation><affiliation><mods:affiliation>Laboratoire de Phytomorphogenèse — UA 45, Biologie Physiologie Végétales, Université Blaise Pascal (Clermont II), 4, rue Ledru, 63038 Clermont-Ferrand, France</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:4DCC6B1D18791F89D255959492976DB9B58FB89B</idno><date when="1988" year="1988">1988</date><idno type="doi">10.1016/0168-9452(88)90054-4</idno><idno type="url">https://api.istex.fr/document/4DCC6B1D18791F89D255959492976DB9B58FB89B/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">000B49</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">Jerusalem artichoke invertases—Immunocharacterization of a soluble form and its putative precursor</title><author><name sortKey="Goupil, P" sort="Goupil, P" uniqKey="Goupil P" first="P." last="Goupil">P. Goupil</name><affiliation><mods:affiliation>Laboratoire de Phytomorphogenèse — UA 45, Biologie Physiologie Végétales, Université Blaise Pascal (Clermont II), 4, rue Ledru, 63038 Clermont-Ferrand, France</mods:affiliation></affiliation></author><author><name sortKey="Croisille, Y" sort="Croisille, Y" uniqKey="Croisille Y" first="Y." last="Croisille">Y. Croisille</name><affiliation><mods:affiliation>Laboratoire de Biologie Animale — UA 677, Embryologie, Sexualité et Endocrinologie, Université Blaise Pascal (Clermont II), Complexe des Cézeaux, 24, avenue des Landais, 63170 Aubière France</mods:affiliation></affiliation></author><author><name sortKey="Croisille, F" sort="Croisille, F" uniqKey="Croisille F" first="F." last="Croisille">F. Croisille</name><affiliation><mods:affiliation>Laboratoire de Biologie Animale — UA 677, Embryologie, Sexualité et Endocrinologie, Université Blaise Pascal (Clermont II), Complexe des Cézeaux, 24, avenue des Landais, 63170 Aubière France</mods:affiliation></affiliation></author><author><name sortKey="Ledoigt, G" sort="Ledoigt, G" uniqKey="Ledoigt G" first="G." last="Ledoigt">G. Ledoigt</name><affiliation><mods:affiliation>To whom correspondence should be sent.</mods:affiliation></affiliation><affiliation><mods:affiliation>Laboratoire de Phytomorphogenèse — UA 45, Biologie Physiologie Végétales, Université Blaise Pascal (Clermont II), 4, rue Ledru, 63038 Clermont-Ferrand, France</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Plant Science</title><title level="j" type="abbrev">PSL</title><idno type="ISSN">0168-9452</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1988">1988</date><biblScope unit="volume">54</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="45">45</biblScope><biblScope unit="page" to="54">54</biblScope></imprint><idno type="ISSN">0168-9452</idno></series><idno type="istex">4DCC6B1D18791F89D255959492976DB9B58FB89B</idno><idno type="DOI">10.1016/0168-9452(88)90054-4</idno><idno type="PII">0168-9452(88)90054-4</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0168-9452</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Using AcA 22 Ultrogel immobilized anti-yeast invertase antibodies a soluble acid invertase (β D fructofuranoside fructohydrolase, EC 3.2.1.26), representing only part of the total acid invertase activity, has been purified from Helianthus tuberosus shoot extracts. Under denaturing conditions (SDS-PAGE) this enzyme usually yields a 58 kDa polypeptide. From one particular extract out of nine, however, a second acid invertase form, yielding essentially a 30 kDa polypeptide, was obtained. Furthermore, after in vitro translation of either polysomal RNA followed by immunoprecipitation, or mRNA isolated from previously immunoselected polysomes, a 97 kDa polypeptide which could be the precursor of both acid invertase forms was observed. The possible physiological significance of these observations is discussed.</div></front></TEI><istex><corpusName>elsevier</corpusName><author><json:item><name>P. Goupil</name><affiliations><json:string>Laboratoire de Phytomorphogenèse — UA 45, Biologie Physiologie Végétales, Université Blaise Pascal (Clermont II), 4, rue Ledru, 63038 Clermont-Ferrand, France</json:string></affiliations></json:item><json:item><name>Y. Croisille</name><affiliations><json:string>Laboratoire de Biologie Animale — UA 677, Embryologie, Sexualité et Endocrinologie, Université Blaise Pascal (Clermont II), Complexe des Cézeaux, 24, avenue des Landais, 63170 Aubière France</json:string></affiliations></json:item><json:item><name>F. Croisille</name><affiliations><json:string>Laboratoire de Biologie Animale — UA 677, Embryologie, Sexualité et Endocrinologie, Université Blaise Pascal (Clermont II), Complexe des Cézeaux, 24, avenue des Landais, 63170 Aubière France</json:string></affiliations></json:item><json:item><name>G. Ledoigt</name><affiliations><json:string>To whom correspondence should be sent.</json:string><json:string>Laboratoire de Phytomorphogenèse — UA 45, Biologie Physiologie Végétales, Université Blaise Pascal (Clermont II), 4, rue Ledru, 63038 Clermont-Ferrand, France</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Helianthus</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>invertase</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>immunoselection</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>invertase biosynthesis</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>polysomes</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>BSA, bovine serum albumin</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Hepes, 4-(2-hydroxyethyl)-1-piperazineethanesulphonic acid</value></json:item></subject><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Using AcA 22 Ultrogel immobilized anti-yeast invertase antibodies a soluble acid invertase (β D fructofuranoside fructohydrolase, EC 3.2.1.26), representing only part of the total acid invertase activity, has been purified from Helianthus tuberosus shoot extracts. Under denaturing conditions (SDS-PAGE) this enzyme usually yields a 58 kDa polypeptide. From one particular extract out of nine, however, a second acid invertase form, yielding essentially a 30 kDa polypeptide, was obtained. Furthermore, after in vitro translation of either polysomal RNA followed by immunoprecipitation, or mRNA isolated from previously immunoselected polysomes, a 97 kDa polypeptide which could be the precursor of both acid invertase forms was observed. 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Under denaturing conditions (SDS-PAGE) this enzyme usually yields a 58 kDa polypeptide. From one particular extract out of nine, however, a second acid invertase form, yielding essentially a 30 kDa polypeptide, was obtained. Furthermore, after in vitro translation of either polysomal RNA followed by immunoprecipitation, or mRNA isolated from previously immunoselected polysomes, a 97 kDa polypeptide which could be the precursor of both acid invertase forms was observed. The possible physiological significance of these observations is discussed.</p></abstract><textClass><keywords scheme="keyword"><list><head>Keywords</head><item><term>Helianthus</term></item><item><term>invertase</term></item><item><term>immunoselection</term></item><item><term>invertase biosynthesis</term></item><item><term>polysomes</term></item></list></keywords></textClass><textClass><keywords scheme="keyword"><list><head>Abbreviations</head><item><term>BSA, bovine serum albumin</term></item><item><term>Hepes, 4-(2-hydroxyethyl)-1-piperazineethanesulphonic acid</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1987-08-25">Modified</change><change when="1988">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><original>false</original><mimetype>text/plain</mimetype><extension>txt</extension><uri>https://api.istex.fr/document/4DCC6B1D18791F89D255959492976DB9B58FB89B/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>PSL</jid><aid>88900544</aid><ce:pii>0168-9452(88)90054-4</ce:pii><ce:doi>10.1016/0168-9452(88)90054-4</ce:doi><ce:copyright type="unknown" year="1988"></ce:copyright></item-info><head><ce:title>Jerusalem artichoke invertases—Immunocharacterization of a soluble form and its putative precursor</ce:title><ce:author-group><ce:author><ce:given-name>P.</ce:given-name><ce:surname>Goupil</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Y.</ce:given-name><ce:surname>Croisille</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>b</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>F.</ce:given-name><ce:surname>Croisille</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>b</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>G.</ce:given-name><ce:surname>Ledoigt</ce:surname><ce:cross-ref refid="COR1"><ce:sup>∗</ce:sup></ce:cross-ref><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:affiliation id="AFF1"><ce:label>a</ce:label><ce:textfn>Laboratoire de Phytomorphogenèse — UA 45, Biologie Physiologie Végétales, Université Blaise Pascal (Clermont II), 4, rue Ledru, 63038 Clermont-Ferrand, France</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>b</ce:label><ce:textfn>Laboratoire de Biologie Animale — UA 677, Embryologie, Sexualité et Endocrinologie, Université Blaise Pascal (Clermont II), Complexe des Cézeaux, 24, avenue des Landais, 63170 Aubière France</ce:textfn></ce:affiliation><ce:correspondence id="COR1"><ce:label>∗</ce:label><ce:text>To whom correspondence should be sent.</ce:text></ce:correspondence></ce:author-group><ce:date-received day="5" month="2" year="1987"></ce:date-received><ce:date-revised day="25" month="8" year="1987"></ce:date-revised><ce:date-accepted day="10" month="9" year="1987"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>Using AcA 22 Ultrogel immobilized anti-yeast invertase antibodies a soluble acid invertase (β D fructofuranoside fructohydrolase, EC 3.2.1.26), representing only part of the total acid invertase activity, has been purified from <ce:italic>Helianthus tuberosus</ce:italic> shoot extracts. Under denaturing conditions (SDS-PAGE) this enzyme usually yields a 58 kDa polypeptide. From one particular extract out of nine, however, a second acid invertase form, yielding essentially a 30 kDa polypeptide, was obtained. Furthermore, after in vitro translation of either polysomal RNA followed by immunoprecipitation, or mRNA isolated from previously immunoselected polysomes, a 97 kDa polypeptide which could be the precursor of both acid invertase forms was observed. The possible physiological significance of these observations is discussed.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text><ce:italic>Helianthus</ce:italic></ce:text></ce:keyword><ce:keyword><ce:text>invertase</ce:text></ce:keyword><ce:keyword><ce:text>immunoselection</ce:text></ce:keyword><ce:keyword><ce:text>invertase biosynthesis</ce:text></ce:keyword><ce:keyword><ce:text>polysomes</ce:text></ce:keyword></ce:keywords><ce:keywords class="abr"><ce:section-title>Abbreviations</ce:section-title><ce:keyword><ce:text>BSA, bovine serum albumin</ce:text></ce:keyword><ce:keyword><ce:text>Hepes, 4-(2-hydroxyethyl)-1-piperazineethanesulphonic acid</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Jerusalem artichoke invertases—Immunocharacterization of a soluble form and its putative precursor</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Jerusalem artichoke invertases—Immunocharacterization of a soluble form and its putative precursor</title></titleInfo><name type="personal"><namePart type="given">P.</namePart><namePart type="family">Goupil</namePart><affiliation>Laboratoire de Phytomorphogenèse — UA 45, Biologie Physiologie Végétales, Université Blaise Pascal (Clermont II), 4, rue Ledru, 63038 Clermont-Ferrand, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Y.</namePart><namePart type="family">Croisille</namePart><affiliation>Laboratoire de Biologie Animale — UA 677, Embryologie, Sexualité et Endocrinologie, Université Blaise Pascal (Clermont II), Complexe des Cézeaux, 24, avenue des Landais, 63170 Aubière France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">F.</namePart><namePart type="family">Croisille</namePart><affiliation>Laboratoire de Biologie Animale — UA 677, Embryologie, Sexualité et Endocrinologie, Université Blaise Pascal (Clermont II), Complexe des Cézeaux, 24, avenue des Landais, 63170 Aubière France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">G.</namePart><namePart type="family">Ledoigt</namePart><affiliation>To whom correspondence should be sent.</affiliation><affiliation>Laboratoire de Phytomorphogenèse — UA 45, Biologie Physiologie Végétales, Université Blaise Pascal (Clermont II), 4, rue Ledru, 63038 Clermont-Ferrand, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article"></genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1988</dateIssued><dateModified encoding="w3cdtf">1987-08-25</dateModified><copyrightDate encoding="w3cdtf">1988</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType></physicalDescription><abstract lang="en">Using AcA 22 Ultrogel immobilized anti-yeast invertase antibodies a soluble acid invertase (β D fructofuranoside fructohydrolase, EC 3.2.1.26), representing only part of the total acid invertase activity, has been purified from Helianthus tuberosus shoot extracts. Under denaturing conditions (SDS-PAGE) this enzyme usually yields a 58 kDa polypeptide. From one particular extract out of nine, however, a second acid invertase form, yielding essentially a 30 kDa polypeptide, was obtained. Furthermore, after in vitro translation of either polysomal RNA followed by immunoprecipitation, or mRNA isolated from previously immunoselected polysomes, a 97 kDa polypeptide which could be the precursor of both acid invertase forms was observed. The possible physiological significance of these observations is discussed.</abstract><subject><genre>Keywords</genre><topic>Helianthus</topic><topic>invertase</topic><topic>immunoselection</topic><topic>invertase biosynthesis</topic><topic>polysomes</topic></subject><subject><genre>Abbreviations</genre><topic>BSA, bovine serum albumin</topic><topic>Hepes, 4-(2-hydroxyethyl)-1-piperazineethanesulphonic acid</topic></subject><relatedItem type="host"><titleInfo><title>Plant Science</title></titleInfo><titleInfo type="abbreviated"><title>PSL</title></titleInfo><genre type="journal">journal</genre><originInfo><dateIssued encoding="w3cdtf">1988</dateIssued></originInfo><identifier type="ISSN">0168-9452</identifier><identifier type="PII">S0168-9452(00)X0164-1</identifier><part><date>1988</date><detail type="volume"><number>54</number><caption>vol.</caption></detail><detail type="issue"><number>1</number><caption>no.</caption></detail><extent unit="issue pages"><start>1</start><end>91</end></extent><extent unit="pages"><start>45</start><end>54</end></extent></part></relatedItem><identifier type="istex">4DCC6B1D18791F89D255959492976DB9B58FB89B</identifier><identifier type="DOI">10.1016/0168-9452(88)90054-4</identifier><identifier type="PII">0168-9452(88)90054-4</identifier><recordInfo><recordContentSource>ELSEVIER</recordContentSource></recordInfo></mods></metadata><enrichments><istex:catWosTEI uri="https://api.istex.fr/document/4DCC6B1D18791F89D255959492976DB9B58FB89B/enrichments/catWos"><teiHeader><profileDesc><textClass><classCode scheme="WOS">BIOCHEMISTRY & MOLECULAR BIOLOGY</classCode><classCode scheme="WOS">PLANT SCIENCES</classCode></textClass></profileDesc></teiHeader></istex:catWosTEI></enrichments></istex></record>Pour manipuler ce document sous Unix (Dilib)
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