Purification of chinook salmon ( Oncorhynchus tshawytscha ) GH for receptor study
Identifieur interne : 000811 ( Istex/Corpus ); précédent : 000810; suivant : 000812Purification of chinook salmon ( Oncorhynchus tshawytscha ) GH for receptor study
Auteurs : Pierre-Yves Le Bail ; Geneviève Boulard ; Bruno Barenton ; Michel ZygmuntSource :
- Fish Physiology and Biochemistry [ 0920-1742 ] ; 1989-06-01.
Abstract
Abstract: A method for the purification of chinook Salmon (Oncorhynchus tshawytscha) GH, which retains its biological activity, is described. The biological activity was investigated with an established radioreceptor assay using liver membranes from pregnant rabbits and bovine GH as standard and labelled hormone. The enrichment of the preparation was checked with electrophoresis (SDS-PAGE). Extraction and further steps were carried out using low molarity alkaline buffer (pH 8–10, M = 100 mM). Three chromatography steps were performed (Concanavalin-A sepharose, Bio-gel P60, DEAE). Ion exchange chromatography was performed under isocratic conditions (using a 50 cm column). Two isoforms (sGH1 and sGH2) were isolated. The purification yield is 0.7% compared to lyophilized pituitaries. The molecule is homogeneous in SDS-PAGE. Contamination by prolactin, gonadotrophin and corticotrophin is negligible (< 0.5%). It could be demonstrated that the biological activity of the preparation is maintained since this preparation stimulates the growth of juvenile trout (Salmo gairdneri) and binds specifically (35%) to trout liver membranes.
Url:
DOI: 10.1007/BF00004713
Links to Exploration step
ISTEX:F531E59BF8B1AEA0C755AA4FB9028AE526BBA863Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Purification of chinook salmon ( Oncorhynchus tshawytscha ) GH for receptor study</title><author><name sortKey="Le Bail, Pierre Yves" sort="Le Bail, Pierre Yves" uniqKey="Le Bail P" first="Pierre-Yves" last="Le Bail">Pierre-Yves Le Bail</name><affiliation><mods:affiliation>Laboratoire de Physiologie des Poissons, INRA, Campus de Beaulieu, 35042, Rennes Cedex, France</mods:affiliation></affiliation></author><author><name sortKey="Boulard, Genevieve" sort="Boulard, Genevieve" uniqKey="Boulard G" first="Geneviève" last="Boulard">Geneviève Boulard</name><affiliation><mods:affiliation>Laboratoire de Physiologie des Poissons, INRA, Campus de Beaulieu, 35042, Rennes Cedex, France</mods:affiliation></affiliation></author><author><name sortKey="Barenton, Bruno" sort="Barenton, Bruno" uniqKey="Barenton B" first="Bruno" last="Barenton">Bruno Barenton</name><affiliation><mods:affiliation>Laboratoire de Physiologie Animale, INRA, 9 place Viala, 34060, Montpellier, France</mods:affiliation></affiliation></author><author><name sortKey="Zygmunt, Michel" sort="Zygmunt, Michel" uniqKey="Zygmunt M" first="Michel" last="Zygmunt">Michel Zygmunt</name><affiliation><mods:affiliation>Station de Pathologie de la Reproduction, INRA, 37380, Nouzilly, France</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:F531E59BF8B1AEA0C755AA4FB9028AE526BBA863</idno><date when="1989" year="1989">1989</date><idno type="doi">10.1007/BF00004713</idno><idno type="url">https://api.istex.fr/document/F531E59BF8B1AEA0C755AA4FB9028AE526BBA863/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">000811</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000811</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Purification of chinook salmon ( Oncorhynchus tshawytscha ) GH for receptor study</title><author><name sortKey="Le Bail, Pierre Yves" sort="Le Bail, Pierre Yves" uniqKey="Le Bail P" first="Pierre-Yves" last="Le Bail">Pierre-Yves Le Bail</name><affiliation><mods:affiliation>Laboratoire de Physiologie des Poissons, INRA, Campus de Beaulieu, 35042, Rennes Cedex, France</mods:affiliation></affiliation></author><author><name sortKey="Boulard, Genevieve" sort="Boulard, Genevieve" uniqKey="Boulard G" first="Geneviève" last="Boulard">Geneviève Boulard</name><affiliation><mods:affiliation>Laboratoire de Physiologie des Poissons, INRA, Campus de Beaulieu, 35042, Rennes Cedex, France</mods:affiliation></affiliation></author><author><name sortKey="Barenton, Bruno" sort="Barenton, Bruno" uniqKey="Barenton B" first="Bruno" last="Barenton">Bruno Barenton</name><affiliation><mods:affiliation>Laboratoire de Physiologie Animale, INRA, 9 place Viala, 34060, Montpellier, France</mods:affiliation></affiliation></author><author><name sortKey="Zygmunt, Michel" sort="Zygmunt, Michel" uniqKey="Zygmunt M" first="Michel" last="Zygmunt">Michel Zygmunt</name><affiliation><mods:affiliation>Station de Pathologie de la Reproduction, INRA, 37380, Nouzilly, France</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Fish Physiology and Biochemistry</title><title level="j" type="abbrev">Fish Physiol Biochem</title><idno type="ISSN">0920-1742</idno><idno type="eISSN">1573-5168</idno><imprint><publisher>Kluwer Academic Publishers</publisher><pubPlace>Dordrecht</pubPlace><date type="published" when="1989-06-01">1989-06-01</date><biblScope unit="volume">7</biblScope><biblScope unit="issue">1-6</biblScope><biblScope unit="page" from="243">243</biblScope><biblScope unit="page" to="251">251</biblScope></imprint><idno type="ISSN">0920-1742</idno></series><idno type="istex">F531E59BF8B1AEA0C755AA4FB9028AE526BBA863</idno><idno type="DOI">10.1007/BF00004713</idno><idno type="ArticleID">BF00004713</idno><idno type="ArticleID">Art31</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0920-1742</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: A method for the purification of chinook Salmon (Oncorhynchus tshawytscha) GH, which retains its biological activity, is described. The biological activity was investigated with an established radioreceptor assay using liver membranes from pregnant rabbits and bovine GH as standard and labelled hormone. The enrichment of the preparation was checked with electrophoresis (SDS-PAGE). Extraction and further steps were carried out using low molarity alkaline buffer (pH 8–10, M = 100 mM). Three chromatography steps were performed (Concanavalin-A sepharose, Bio-gel P60, DEAE). Ion exchange chromatography was performed under isocratic conditions (using a 50 cm column). Two isoforms (sGH1 and sGH2) were isolated. The purification yield is 0.7% compared to lyophilized pituitaries. The molecule is homogeneous in SDS-PAGE. Contamination by prolactin, gonadotrophin and corticotrophin is negligible (< 0.5%). It could be demonstrated that the biological activity of the preparation is maintained since this preparation stimulates the growth of juvenile trout (Salmo gairdneri) and binds specifically (35%) to trout liver membranes.</div></front></TEI><istex><corpusName>springer</corpusName><author><json:item><name>Pierre-Yves Le Bail</name><affiliations><json:string>Laboratoire de Physiologie des Poissons, INRA, Campus de Beaulieu, 35042, Rennes Cedex, France</json:string></affiliations></json:item><json:item><name>Geneviève Boulard</name><affiliations><json:string>Laboratoire de Physiologie des Poissons, INRA, Campus de Beaulieu, 35042, Rennes Cedex, France</json:string></affiliations></json:item><json:item><name>Bruno Barenton</name><affiliations><json:string>Laboratoire de Physiologie Animale, INRA, 9 place Viala, 34060, Montpellier, France</json:string></affiliations></json:item><json:item><name>Michel Zygmunt</name><affiliations><json:string>Station de Pathologie de la Reproduction, INRA, 37380, Nouzilly, France</json:string></affiliations></json:item></author><articleId><json:string>BF00004713</json:string><json:string>Art31</json:string></articleId><language><json:string>eng</json:string></language><originalGenre><json:string>OriginalPaper</json:string></originalGenre><abstract>Abstract: A method for the purification of chinook Salmon (Oncorhynchus tshawytscha) GH, which retains its biological activity, is described. The biological activity was investigated with an established radioreceptor assay using liver membranes from pregnant rabbits and bovine GH as standard and labelled hormone. The enrichment of the preparation was checked with electrophoresis (SDS-PAGE). Extraction and further steps were carried out using low molarity alkaline buffer (pH 8–10, M = 100 mM). Three chromatography steps were performed (Concanavalin-A sepharose, Bio-gel P60, DEAE). Ion exchange chromatography was performed under isocratic conditions (using a 50 cm column). Two isoforms (sGH1 and sGH2) were isolated. The purification yield is 0.7% compared to lyophilized pituitaries. The molecule is homogeneous in SDS-PAGE. Contamination by prolactin, gonadotrophin and corticotrophin is negligible (> 0.5%). It could be demonstrated that the biological activity of the preparation is maintained since this preparation stimulates the growth of juvenile trout (Salmo gairdneri) and binds specifically (35%) to trout liver membranes.</abstract><qualityIndicators><score>5.561</score><pdfVersion>1.3</pdfVersion><pdfPageSize>540 x 738 pts</pdfPageSize><refBibsNative>false</refBibsNative><keywordCount>0</keywordCount><abstractCharCount>1140</abstractCharCount><pdfWordCount>3665</pdfWordCount><pdfCharCount>22686</pdfCharCount><pdfPageCount>9</pdfPageCount><abstractWordCount>158</abstractWordCount></qualityIndicators><title>Purification of chinook salmon ( Oncorhynchus tshawytscha ) GH for receptor study</title><genre><json:string>research-article</json:string></genre><host><volume>7</volume><pages><last>251</last><first>243</first></pages><issn><json:string>0920-1742</json:string></issn><issue>1-6</issue><subject><json:item><value>Animal Biochemistry</value></json:item><json:item><value>Hydrobiology</value></json:item><json:item><value>Zoology</value></json:item><json:item><value>Animal Anatomy / Morphology / Histology</value></json:item><json:item><value>Animal Physiology</value></json:item></subject><journalId><json:string>10695</json:string></journalId><genre><json:string>journal</json:string></genre><language><json:string>unknown</json:string></language><eissn><json:string>1573-5168</json:string></eissn><title>Fish Physiology and Biochemistry</title><publicationDate>1989</publicationDate><copyrightDate>1989</copyrightDate></host><categories><wos><json:string>science</json:string><json:string>physiology</json:string><json:string>fisheries</json:string><json:string>biochemistry & molecular biology</json:string></wos><scienceMetrix><json:string>applied sciences</json:string><json:string>agriculture, fisheries & forestry</json:string><json:string>fisheries</json:string></scienceMetrix></categories><publicationDate>1989</publicationDate><copyrightDate>1989</copyrightDate><doi><json:string>10.1007/BF00004713</json:string></doi><id>F531E59BF8B1AEA0C755AA4FB9028AE526BBA863</id><score>0.029163158</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/document/F531E59BF8B1AEA0C755AA4FB9028AE526BBA863/fulltext/pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/document/F531E59BF8B1AEA0C755AA4FB9028AE526BBA863/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/F531E59BF8B1AEA0C755AA4FB9028AE526BBA863/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">Purification of chinook salmon ( Oncorhynchus tshawytscha ) GH for receptor study</title><respStmt><resp>Références bibliographiques récupérées via GROBID</resp><name resp="ISTEX-API">ISTEX-API (INIST-CNRS)</name></respStmt><respStmt><resp>Références bibliographiques récupérées via GROBID</resp><name resp="ISTEX-API">ISTEX-API (INIST-CNRS)</name></respStmt></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>Kluwer Academic Publishers</publisher><pubPlace>Dordrecht</pubPlace><availability><p>Kugler Publications, 1989</p></availability><date>1989</date></publicationStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">Purification of chinook salmon ( Oncorhynchus tshawytscha ) GH for receptor study</title><author xml:id="author-1"><persName><forename type="first">Pierre-Yves</forename><surname>Le Bail</surname></persName><affiliation>Laboratoire de Physiologie des Poissons, INRA, Campus de Beaulieu, 35042, Rennes Cedex, France</affiliation></author><author xml:id="author-2"><persName><forename type="first">Geneviève</forename><surname>Boulard</surname></persName><affiliation>Laboratoire de Physiologie des Poissons, INRA, Campus de Beaulieu, 35042, Rennes Cedex, France</affiliation></author><author xml:id="author-3"><persName><forename type="first">Bruno</forename><surname>Barenton</surname></persName><affiliation>Laboratoire de Physiologie Animale, INRA, 9 place Viala, 34060, Montpellier, France</affiliation></author><author xml:id="author-4"><persName><forename type="first">Michel</forename><surname>Zygmunt</surname></persName><affiliation>Station de Pathologie de la Reproduction, INRA, 37380, Nouzilly, France</affiliation></author></analytic><monogr><title level="j">Fish Physiology and Biochemistry</title><title level="j" type="abbrev">Fish Physiol Biochem</title><idno type="journal-ID">10695</idno><idno type="pISSN">0920-1742</idno><idno type="eISSN">1573-5168</idno><idno type="issue-article-count">56</idno><idno type="volume-issue-count">6</idno><imprint><publisher>Kluwer Academic Publishers</publisher><pubPlace>Dordrecht</pubPlace><date type="published" when="1989-06-01"></date><biblScope unit="volume">7</biblScope><biblScope unit="issue">1-6</biblScope><biblScope unit="page" from="243">243</biblScope><biblScope unit="page" to="251">251</biblScope></imprint></monogr><idno type="istex">F531E59BF8B1AEA0C755AA4FB9028AE526BBA863</idno><idno type="DOI">10.1007/BF00004713</idno><idno type="ArticleID">BF00004713</idno><idno type="ArticleID">Art31</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1989</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Abstract: A method for the purification of chinook Salmon (Oncorhynchus tshawytscha) GH, which retains its biological activity, is described. The biological activity was investigated with an established radioreceptor assay using liver membranes from pregnant rabbits and bovine GH as standard and labelled hormone. The enrichment of the preparation was checked with electrophoresis (SDS-PAGE). Extraction and further steps were carried out using low molarity alkaline buffer (pH 8–10, M = 100 mM). Three chromatography steps were performed (Concanavalin-A sepharose, Bio-gel P60, DEAE). Ion exchange chromatography was performed under isocratic conditions (using a 50 cm column). Two isoforms (sGH1 and sGH2) were isolated. The purification yield is 0.7% compared to lyophilized pituitaries. The molecule is homogeneous in SDS-PAGE. Contamination by prolactin, gonadotrophin and corticotrophin is negligible (< 0.5%). It could be demonstrated that the biological activity of the preparation is maintained since this preparation stimulates the growth of juvenile trout (Salmo gairdneri) and binds specifically (35%) to trout liver membranes.</p></abstract><textClass><keywords scheme="Journal Subject"><list><head>Life Sciences</head><item><term>Animal Biochemistry</term></item><item><term>Hydrobiology</term></item><item><term>Zoology</term></item><item><term>Animal Anatomy / Morphology / Histology</term></item><item><term>Animal Physiology</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1989-06-01">Published</change><change xml:id="refBibs-istex" who="#ISTEX-API" when="2016-11-23">References added</change><change xml:id="refBibs-istex" who="#ISTEX-API" when="2017-01-21">References added</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/F531E59BF8B1AEA0C755AA4FB9028AE526BBA863/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Springer, Publisher found" wicri:toSee="no header"><istex:xmlDeclaration>version="1.0" encoding="UTF-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//Springer-Verlag//DTD A++ V2.4//EN" URI="http://devel.springer.de/A++/V2.4/DTD/A++V2.4.dtd" name="istex:docType"></istex:docType><istex:document><Publisher><PublisherInfo><PublisherName>Kluwer Academic Publishers</PublisherName><PublisherLocation>Dordrecht</PublisherLocation></PublisherInfo><Journal><JournalInfo JournalProductType="ArchiveJournal" NumberingStyle="Unnumbered"><JournalID>10695</JournalID><JournalPrintISSN>0920-1742</JournalPrintISSN><JournalElectronicISSN>1573-5168</JournalElectronicISSN><JournalTitle>Fish Physiology and Biochemistry</JournalTitle><JournalAbbreviatedTitle>Fish Physiol Biochem</JournalAbbreviatedTitle><JournalSubjectGroup><JournalSubject Type="Primary">Life Sciences</JournalSubject><JournalSubject Type="Secondary">Animal Biochemistry</JournalSubject><JournalSubject Type="Secondary">Hydrobiology</JournalSubject><JournalSubject Type="Secondary">Zoology</JournalSubject><JournalSubject Type="Secondary">Animal Anatomy / Morphology / Histology</JournalSubject><JournalSubject Type="Secondary">Animal Physiology</JournalSubject></JournalSubjectGroup></JournalInfo><Volume><VolumeInfo TocLevels="0" VolumeType="Regular"><VolumeIDStart>7</VolumeIDStart><VolumeIDEnd>7</VolumeIDEnd><VolumeIssueCount>6</VolumeIssueCount></VolumeInfo><Issue IssueType="Combined"><IssueInfo TocLevels="0"><IssueIDStart>1</IssueIDStart><IssueIDEnd>6</IssueIDEnd><IssueArticleCount>56</IssueArticleCount><IssueHistory><CoverDate><Year>1989</Year><Month>6</Month></CoverDate></IssueHistory><IssueCopyright><CopyrightHolderName>Kugler Publications</CopyrightHolderName><CopyrightYear>1989</CopyrightYear></IssueCopyright></IssueInfo><Article ID="Art31"><ArticleInfo ArticleType="OriginalPaper" ContainsESM="No" Language="En" NumberingStyle="Unnumbered" TocLevels="0"><ArticleID>BF00004713</ArticleID><ArticleDOI>10.1007/BF00004713</ArticleDOI><ArticleSequenceNumber>31</ArticleSequenceNumber><ArticleTitle Language="En">Purification of chinook salmon (<Emphasis Type="Italic">Oncorhynchus tshawytscha</Emphasis>) GH for receptor study</ArticleTitle><ArticleFirstPage>243</ArticleFirstPage><ArticleLastPage>251</ArticleLastPage><ArticleHistory><RegistrationDate><Year>2004</Year><Month>3</Month><Day>26</Day></RegistrationDate></ArticleHistory><ArticleCopyright><CopyrightHolderName>Kugler Publications</CopyrightHolderName><CopyrightYear>1989</CopyrightYear></ArticleCopyright><ArticleGrants Type="Regular"><MetadataGrant Grant="OpenAccess"></MetadataGrant><AbstractGrant Grant="OpenAccess"></AbstractGrant><BodyPDFGrant Grant="Restricted"></BodyPDFGrant><BodyHTMLGrant Grant="Restricted"></BodyHTMLGrant><BibliographyGrant Grant="Restricted"></BibliographyGrant><ESMGrant Grant="Restricted"></ESMGrant></ArticleGrants><ArticleContext><JournalID>10695</JournalID><VolumeIDStart>7</VolumeIDStart><VolumeIDEnd>7</VolumeIDEnd><IssueIDStart>1</IssueIDStart><IssueIDEnd>6</IssueIDEnd></ArticleContext></ArticleInfo><ArticleHeader><AuthorGroup><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Pierre-Yves</GivenName><Particle>Le</Particle><FamilyName>Bail</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Geneviève</GivenName><FamilyName>Boulard</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff2"><AuthorName DisplayOrder="Western"><GivenName>Bruno</GivenName><FamilyName>Barenton</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff3"><AuthorName DisplayOrder="Western"><GivenName>Michel</GivenName><FamilyName>Zygmunt</FamilyName></AuthorName></Author><Affiliation ID="Aff1"><OrgDivision>Laboratoire de Physiologie des Poissons, INRA</OrgDivision><OrgName>Campus de Beaulieu</OrgName><OrgAddress><Postcode>35042</Postcode><City>Rennes Cedex</City><Country>France</Country></OrgAddress></Affiliation><Affiliation ID="Aff2"><OrgDivision>Laboratoire de Physiologie Animale</OrgDivision><OrgName>INRA</OrgName><OrgAddress><Street>9 place Viala</Street><Postcode>34060</Postcode><City>Montpellier</City><Country>France</Country></OrgAddress></Affiliation><Affiliation ID="Aff3"><OrgDivision>Station de Pathologie de la Reproduction</OrgDivision><OrgName>INRA</OrgName><OrgAddress><Postcode>37380</Postcode><City>Nouzilly</City><Country>France</Country></OrgAddress></Affiliation></AuthorGroup><Abstract ID="Abs1" Language="En"><Heading>Abstract</Heading><Para>A method for the purification of chinook Salmon (<Emphasis Type="Italic">Oncorhynchus tshawytscha</Emphasis>) GH, which retains its biological activity, is described. The biological activity was investigated with an established radioreceptor assay using liver membranes from pregnant rabbits and bovine GH as standard and labelled hormone. The enrichment of the preparation was checked with electrophoresis (SDS-PAGE). Extraction and further steps were carried out using low molarity alkaline buffer (pH 8–10, M = 100 mM). Three chromatography steps were performed (Concanavalin-A sepharose, Bio-gel P60, DEAE). Ion exchange chromatography was performed under isocratic conditions (using a 50 cm column). Two isoforms (sGH1 and sGH2) were isolated. The purification yield is 0.7% compared to lyophilized pituitaries. The molecule is homogeneous in SDS-PAGE. Contamination by prolactin, gonadotrophin and corticotrophin is negligible (< 0.5%). It could be demonstrated that the biological activity of the preparation is maintained since this preparation stimulates the growth of juvenile trout (<Emphasis Type="Italic">Salmo gairdneri</Emphasis>) and binds specifically (35%) to trout liver membranes.</Para></Abstract><KeywordGroup Language="En"><Heading>Keywords</Heading><Keyword>fish</Keyword><Keyword>salmon</Keyword><Keyword>growth hormone</Keyword><Keyword>biological activity</Keyword><Keyword>radioreceptor assay</Keyword><Keyword>purification techniques</Keyword></KeywordGroup></ArticleHeader><NoBody></NoBody></Article></Issue></Volume></Journal></Publisher></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Purification of chinook salmon ( Oncorhynchus tshawytscha ) GH for receptor study</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Purification of chinook salmon (Oncorhynchus tshawytscha) GH for receptor study</title></titleInfo><name type="personal"><namePart type="given">Pierre-Yves</namePart><namePart type="family">Le Bail</namePart><affiliation>Laboratoire de Physiologie des Poissons, INRA, Campus de Beaulieu, 35042, Rennes Cedex, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Geneviève</namePart><namePart type="family">Boulard</namePart><affiliation>Laboratoire de Physiologie des Poissons, INRA, Campus de Beaulieu, 35042, Rennes Cedex, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Bruno</namePart><namePart type="family">Barenton</namePart><affiliation>Laboratoire de Physiologie Animale, INRA, 9 place Viala, 34060, Montpellier, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Michel</namePart><namePart type="family">Zygmunt</namePart><affiliation>Station de Pathologie de la Reproduction, INRA, 37380, Nouzilly, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="OriginalPaper"></genre><originInfo><publisher>Kluwer Academic Publishers</publisher><place><placeTerm type="text">Dordrecht</placeTerm></place><dateIssued encoding="w3cdtf">1989-06-01</dateIssued><copyrightDate encoding="w3cdtf">1989</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType></physicalDescription><abstract lang="en">Abstract: A method for the purification of chinook Salmon (Oncorhynchus tshawytscha) GH, which retains its biological activity, is described. The biological activity was investigated with an established radioreceptor assay using liver membranes from pregnant rabbits and bovine GH as standard and labelled hormone. The enrichment of the preparation was checked with electrophoresis (SDS-PAGE). Extraction and further steps were carried out using low molarity alkaline buffer (pH 8–10, M = 100 mM). Three chromatography steps were performed (Concanavalin-A sepharose, Bio-gel P60, DEAE). Ion exchange chromatography was performed under isocratic conditions (using a 50 cm column). Two isoforms (sGH1 and sGH2) were isolated. The purification yield is 0.7% compared to lyophilized pituitaries. The molecule is homogeneous in SDS-PAGE. Contamination by prolactin, gonadotrophin and corticotrophin is negligible (< 0.5%). It could be demonstrated that the biological activity of the preparation is maintained since this preparation stimulates the growth of juvenile trout (Salmo gairdneri) and binds specifically (35%) to trout liver membranes.</abstract><relatedItem type="host"><titleInfo><title>Fish Physiology and Biochemistry</title></titleInfo><titleInfo type="abbreviated"><title>Fish Physiol Biochem</title></titleInfo><genre type="journal" displayLabel="Archive Journal"></genre><originInfo><dateIssued encoding="w3cdtf">1989-06-01</dateIssued><copyrightDate encoding="w3cdtf">1989</copyrightDate></originInfo><subject><genre>Life Sciences</genre><topic>Animal Biochemistry</topic><topic>Hydrobiology</topic><topic>Zoology</topic><topic>Animal Anatomy / Morphology / Histology</topic><topic>Animal Physiology</topic></subject><identifier type="ISSN">0920-1742</identifier><identifier type="eISSN">1573-5168</identifier><identifier type="JournalID">10695</identifier><identifier type="IssueArticleCount">56</identifier><identifier type="VolumeIssueCount">6</identifier><part><date>1989</date><detail type="volume"><number>7</number><caption>vol.</caption></detail><detail type="issue"><number>1-6</number><caption>no.</caption></detail><extent unit="pages"><start>243</start><end>251</end></extent></part><recordInfo><recordOrigin>Kugler Publications, 1989</recordOrigin></recordInfo></relatedItem><identifier type="istex">F531E59BF8B1AEA0C755AA4FB9028AE526BBA863</identifier><identifier type="DOI">10.1007/BF00004713</identifier><identifier type="ArticleID">BF00004713</identifier><identifier type="ArticleID">Art31</identifier><accessCondition type="use and reproduction" contentType="copyright">Kugler Publications, 1989</accessCondition><recordInfo><recordContentSource>SPRINGER</recordContentSource><recordOrigin>Kugler Publications, 1989</recordOrigin></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Eau/explor/EsturgeonV1/Data/Istex/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000811 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Istex/Corpus/biblio.hfd -nk 000811 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Wicri/Eau
|area= EsturgeonV1
|flux= Istex
|étape= Corpus
|type= RBID
|clé= ISTEX:F531E59BF8B1AEA0C755AA4FB9028AE526BBA863
|texte= Purification of chinook salmon ( Oncorhynchus tshawytscha ) GH for receptor study
}}
| This area was generated with Dilib version V0.6.27. |  |