Mammalian gonadotropin-releasing hormone (GnRH) identified by primary structure in Russian sturgeon, Acipenser gueldenstaedti
Identifieur interne : 000A21 ( Istex/Corpus ); précédent : 000A20; suivant : 000A22Mammalian gonadotropin-releasing hormone (GnRH) identified by primary structure in Russian sturgeon, Acipenser gueldenstaedti
Auteurs : D. W. Lescheid ; J. F. F. Powell ; W. H. Fischer ; M. Park ; A. Craig ; O. Bukovskaya ; I. A. Barannikova ; N. M. SherwoodSource :
- Regulatory Peptides [ 0167-0115 ] ; 1995.
Abstract
The mammalian form of gonadotropin-releasing hormone (GnRH) was purified from the brains of Russian sturgeon, Acipenser gueldenstaedti, using reversed-phase high pressure liquid chromatography (HPLC). The total concentration of mGnRH within these fish was 5.4 ng/brain. Small amounts of immunoreactive chicken GnRH-II like molecules were also detected but at insufficient quantities for purification. The primary structure of mGnRH was determined using automated Edman degradation. Because sequence data could not be obtained until after digestion by bovine pyroglutamyl aminopeptidase, it was determined that the amino-terminal residue was modified. Furthermore, mass spectrometric data and co-elution with synthetic mGnRH on HPLC confirmed that the carboxy-terminal residue was amidated. The amino acid sequence of sturgeon GnRH is pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2.
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DOI: 10.1016/0167-0115(94)00118-H
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<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title>Mammalian gonadotropin-releasing hormone (GnRH) identified by primary structure in Russian sturgeon, Acipenser gueldenstaedti</title><author><name sortKey="Lescheid, D W" sort="Lescheid, D W" uniqKey="Lescheid D" first="D. W." last="Lescheid">D. W. Lescheid</name><affiliation><mods:affiliation>Department of Biology, University of Victoria, Victoria, B.C., V8W 2Y2, Canada</mods:affiliation></affiliation></author><author><name sortKey="Powell, J F F" sort="Powell, J F F" uniqKey="Powell J" first="J. F. F." last="Powell">J. F. F. Powell</name><affiliation><mods:affiliation>Department of Biology, University of Victoria, Victoria, B.C., V8W 2Y2, Canada</mods:affiliation></affiliation></author><author><name sortKey="Fischer, W H" sort="Fischer, W H" uniqKey="Fischer W" first="W. H." last="Fischer">W. H. Fischer</name><affiliation><mods:affiliation>The Clayton Foundation Laboratories for Peptide Biology, The Salk Institute, La Jolla, CA 92037, USA</mods:affiliation></affiliation></author><author><name sortKey="Park, M" sort="Park, M" uniqKey="Park M" first="M." last="Park">M. Park</name><affiliation><mods:affiliation>The Clayton Foundation Laboratories for Peptide Biology, The Salk Institute, La Jolla, CA 92037, USA</mods:affiliation></affiliation></author><author><name sortKey="Craig, A" sort="Craig, A" uniqKey="Craig A" first="A." last="Craig">A. Craig</name><affiliation><mods:affiliation>The Clayton Foundation Laboratories for Peptide Biology, The Salk Institute, La Jolla, CA 92037, USA</mods:affiliation></affiliation></author><author><name sortKey="Bukovskaya, O" sort="Bukovskaya, O" uniqKey="Bukovskaya O" first="O." last="Bukovskaya">O. Bukovskaya</name><affiliation><mods:affiliation>Physiological Institute, St. Petersburg University, St. Petersburg 199034, Russian Federation</mods:affiliation></affiliation></author><author><name sortKey="Barannikova, I A" sort="Barannikova, I A" uniqKey="Barannikova I" first="I. A." last="Barannikova">I. A. Barannikova</name><affiliation><mods:affiliation>Physiological Institute, St. Petersburg University, St. Petersburg 199034, Russian Federation</mods:affiliation></affiliation></author><author><name sortKey="Sherwood, N M" sort="Sherwood, N M" uniqKey="Sherwood N" first="N. M." last="Sherwood">N. M. Sherwood</name><affiliation><mods:affiliation>Corresponding author.</mods:affiliation></affiliation><affiliation><mods:affiliation>Department of Biology, University of Victoria, Victoria, B.C., V8W 2Y2, Canada</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:EF9B0369BC6ACADB6F0B0A548F4B69C0DEA68AEB</idno><date when="1995" year="1995">1995</date><idno type="doi">10.1016/0167-0115(94)00118-H</idno><idno type="url">https://api.istex.fr/document/EF9B0369BC6ACADB6F0B0A548F4B69C0DEA68AEB/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">000A21</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000A21</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">Mammalian gonadotropin-releasing hormone (GnRH) identified by primary structure in Russian sturgeon, Acipenser gueldenstaedti</title><author><name sortKey="Lescheid, D W" sort="Lescheid, D W" uniqKey="Lescheid D" first="D. W." last="Lescheid">D. W. Lescheid</name><affiliation><mods:affiliation>Department of Biology, University of Victoria, Victoria, B.C., V8W 2Y2, Canada</mods:affiliation></affiliation></author><author><name sortKey="Powell, J F F" sort="Powell, J F F" uniqKey="Powell J" first="J. F. F." last="Powell">J. F. F. Powell</name><affiliation><mods:affiliation>Department of Biology, University of Victoria, Victoria, B.C., V8W 2Y2, Canada</mods:affiliation></affiliation></author><author><name sortKey="Fischer, W H" sort="Fischer, W H" uniqKey="Fischer W" first="W. H." last="Fischer">W. H. Fischer</name><affiliation><mods:affiliation>The Clayton Foundation Laboratories for Peptide Biology, The Salk Institute, La Jolla, CA 92037, USA</mods:affiliation></affiliation></author><author><name sortKey="Park, M" sort="Park, M" uniqKey="Park M" first="M." last="Park">M. Park</name><affiliation><mods:affiliation>The Clayton Foundation Laboratories for Peptide Biology, The Salk Institute, La Jolla, CA 92037, USA</mods:affiliation></affiliation></author><author><name sortKey="Craig, A" sort="Craig, A" uniqKey="Craig A" first="A." last="Craig">A. Craig</name><affiliation><mods:affiliation>The Clayton Foundation Laboratories for Peptide Biology, The Salk Institute, La Jolla, CA 92037, USA</mods:affiliation></affiliation></author><author><name sortKey="Bukovskaya, O" sort="Bukovskaya, O" uniqKey="Bukovskaya O" first="O." last="Bukovskaya">O. Bukovskaya</name><affiliation><mods:affiliation>Physiological Institute, St. Petersburg University, St. Petersburg 199034, Russian Federation</mods:affiliation></affiliation></author><author><name sortKey="Barannikova, I A" sort="Barannikova, I A" uniqKey="Barannikova I" first="I. A." last="Barannikova">I. A. Barannikova</name><affiliation><mods:affiliation>Physiological Institute, St. Petersburg University, St. Petersburg 199034, Russian Federation</mods:affiliation></affiliation></author><author><name sortKey="Sherwood, N M" sort="Sherwood, N M" uniqKey="Sherwood N" first="N. M." last="Sherwood">N. M. Sherwood</name><affiliation><mods:affiliation>Corresponding author.</mods:affiliation></affiliation><affiliation><mods:affiliation>Department of Biology, University of Victoria, Victoria, B.C., V8W 2Y2, Canada</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Regulatory Peptides</title><title level="j" type="abbrev">REGPEP</title><idno type="ISSN">0167-0115</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1995">1995</date><biblScope unit="volume">55</biblScope><biblScope unit="issue">3</biblScope><biblScope unit="page" from="299">299</biblScope><biblScope unit="page" to="309">309</biblScope></imprint><idno type="ISSN">0167-0115</idno></series><idno type="istex">EF9B0369BC6ACADB6F0B0A548F4B69C0DEA68AEB</idno><idno type="DOI">10.1016/0167-0115(94)00118-H</idno><idno type="PII">0167-0115(94)00118-H</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0167-0115</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The mammalian form of gonadotropin-releasing hormone (GnRH) was purified from the brains of Russian sturgeon, Acipenser gueldenstaedti, using reversed-phase high pressure liquid chromatography (HPLC). The total concentration of mGnRH within these fish was 5.4 ng/brain. Small amounts of immunoreactive chicken GnRH-II like molecules were also detected but at insufficient quantities for purification. The primary structure of mGnRH was determined using automated Edman degradation. Because sequence data could not be obtained until after digestion by bovine pyroglutamyl aminopeptidase, it was determined that the amino-terminal residue was modified. Furthermore, mass spectrometric data and co-elution with synthetic mGnRH on HPLC confirmed that the carboxy-terminal residue was amidated. The amino acid sequence of sturgeon GnRH is pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2.</div></front></TEI><istex><corpusName>elsevier</corpusName><author><json:item><name>D.W. Lescheid</name><affiliations><json:string>Department of Biology, University of Victoria, Victoria, B.C., V8W 2Y2, Canada</json:string></affiliations></json:item><json:item><name>J.F.F. Powell</name><affiliations><json:string>Department of Biology, University of Victoria, Victoria, B.C., V8W 2Y2, Canada</json:string></affiliations></json:item><json:item><name>W.H. Fischer</name><affiliations><json:string>The Clayton Foundation Laboratories for Peptide Biology, The Salk Institute, La Jolla, CA 92037, USA</json:string></affiliations></json:item><json:item><name>M. Park</name><affiliations><json:string>The Clayton Foundation Laboratories for Peptide Biology, The Salk Institute, La Jolla, CA 92037, USA</json:string></affiliations></json:item><json:item><name>A. Craig</name><affiliations><json:string>The Clayton Foundation Laboratories for Peptide Biology, The Salk Institute, La Jolla, CA 92037, USA</json:string></affiliations></json:item><json:item><name>O. Bukovskaya</name><affiliations><json:string>Physiological Institute, St. Petersburg University, St. Petersburg 199034, Russian Federation</json:string></affiliations></json:item><json:item><name>I.A. Barannikova</name><affiliations><json:string>Physiological Institute, St. Petersburg University, St. Petersburg 199034, Russian Federation</json:string></affiliations></json:item><json:item><name>N.M. Sherwood</name><affiliations><json:string>Corresponding author.</json:string><json:string>Department of Biology, University of Victoria, Victoria, B.C., V8W 2Y2, Canada</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Reproduction</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Luteinizing hormone-releasing hormone</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Sturgeon</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Fish</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Neuropeptide</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Brain peptide</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Osteichthyes</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Evolution</value></json:item></subject><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>The mammalian form of gonadotropin-releasing hormone (GnRH) was purified from the brains of Russian sturgeon, Acipenser gueldenstaedti, using reversed-phase high pressure liquid chromatography (HPLC). The total concentration of mGnRH within these fish was 5.4 ng/brain. Small amounts of immunoreactive chicken GnRH-II like molecules were also detected but at insufficient quantities for purification. The primary structure of mGnRH was determined using automated Edman degradation. Because sequence data could not be obtained until after digestion by bovine pyroglutamyl aminopeptidase, it was determined that the amino-terminal residue was modified. Furthermore, mass spectrometric data and co-elution with synthetic mGnRH on HPLC confirmed that the carboxy-terminal residue was amidated. The amino acid sequence of sturgeon GnRH is pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2.</abstract><qualityIndicators><score>6.356</score><pdfVersion>1.2</pdfVersion><pdfPageSize>548 x 749 pts</pdfPageSize><refBibsNative>true</refBibsNative><keywordCount>8</keywordCount><abstractCharCount>879</abstractCharCount><pdfWordCount>5089</pdfWordCount><pdfCharCount>31287</pdfCharCount><pdfPageCount>11</pdfPageCount><abstractWordCount>113</abstractWordCount></qualityIndicators><title>Mammalian gonadotropin-releasing hormone (GnRH) identified by primary structure in Russian sturgeon, Acipenser gueldenstaedti</title><pii><json:string>0167-0115(94)00118-H</json:string></pii><genre><json:string>research-article</json:string></genre><serie><volume>69</volume><pages><last>282</last><first>278</first></pages><language><json:string>unknown</json:string></language><title>Proc. Natl. Acad. Sci. 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The total concentration of mGnRH within these fish was 5.4 ng/brain. Small amounts of immunoreactive chicken GnRH-II like molecules were also detected but at insufficient quantities for purification. The primary structure of mGnRH was determined using automated Edman degradation. Because sequence data could not be obtained until after digestion by bovine pyroglutamyl aminopeptidase, it was determined that the amino-terminal residue was modified. Furthermore, mass spectrometric data and co-elution with synthetic mGnRH on HPLC confirmed that the carboxy-terminal residue was amidated. The amino acid sequence of sturgeon GnRH is pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2.</p></abstract><textClass><keywords scheme="keyword"><list><head>Keywords</head><item><term>Reproduction</term></item><item><term>Luteinizing hormone-releasing hormone</term></item><item><term>Sturgeon</term></item><item><term>Fish</term></item><item><term>Neuropeptide</term></item><item><term>Brain peptide</term></item><item><term>Osteichthyes</term></item><item><term>Evolution</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1995">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/EF9B0369BC6ACADB6F0B0A548F4B69C0DEA68AEB/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>REGPEP</jid><aid>9400118H</aid><ce:pii>0167-0115(94)00118-H</ce:pii><ce:doi>10.1016/0167-0115(94)00118-H</ce:doi><ce:copyright type="unknown" year="1995"></ce:copyright></item-info><head><ce:title>Mammalian gonadotropin-releasing hormone (GnRH) identified by primary structure in Russian sturgeon, <ce:italic>Acipenser gueldenstaedti</ce:italic></ce:title><ce:author-group><ce:author><ce:given-name>D.W.</ce:given-name><ce:surname>Lescheid</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>J.F.F.</ce:given-name><ce:surname>Powell</ce:surname><ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>W.H.</ce:given-name><ce:surname>Fischer</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>b</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>M.</ce:given-name><ce:surname>Park</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>b</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>A.</ce:given-name><ce:surname>Craig</ce:surname><ce:cross-ref refid="AFF2"><ce:sup>b</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>O.</ce:given-name><ce:surname>Bukovskaya</ce:surname><ce:cross-ref refid="AFF3"><ce:sup>c</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>I.A.</ce:given-name><ce:surname>Barannikova</ce:surname><ce:cross-ref refid="AFF3"><ce:sup>c</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>N.M.</ce:given-name><ce:surname>Sherwood</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>Department of Biology, University of Victoria, Victoria, B.C., V8W 2Y2, Canada</ce:textfn></ce:affiliation><ce:affiliation id="AFF2"><ce:label>b</ce:label><ce:textfn>The Clayton Foundation Laboratories for Peptide Biology, The Salk Institute, La Jolla, CA 92037, USA</ce:textfn></ce:affiliation><ce:affiliation id="AFF3"><ce:label>c</ce:label><ce:textfn>Physiological Institute, St. Petersburg University, St. Petersburg 199034, Russian Federation</ce:textfn></ce:affiliation><ce:correspondence id="COR1"><ce:label>∗</ce:label><ce:text>Corresponding author.</ce:text></ce:correspondence></ce:author-group><ce:date-received day="24" month="8" year="1994"></ce:date-received><ce:date-accepted day="14" month="11" year="1994"></ce:date-accepted><ce:abstract><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para>The mammalian form of gonadotropin-releasing hormone (GnRH) was purified from the brains of Russian sturgeon, <ce:italic>Acipenser gueldenstaedti</ce:italic>, using reversed-phase high pressure liquid chromatography (HPLC). The total concentration of mGnRH within these fish was 5.4 ng/brain. Small amounts of immunoreactive chicken GnRH-II like molecules were also detected but at insufficient quantities for purification. The primary structure of mGnRH was determined using automated Edman degradation. Because sequence data could not be obtained until after digestion by bovine pyroglutamyl aminopeptidase, it was determined that the amino-terminal residue was modified. Furthermore, mass spectrometric data and co-elution with synthetic mGnRH on HPLC confirmed that the carboxy-terminal residue was amidated. The amino acid sequence of sturgeon GnRH is pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH<ce:inf>2</ce:inf>.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text>Reproduction</ce:text></ce:keyword><ce:keyword><ce:text>Luteinizing hormone-releasing hormone</ce:text></ce:keyword><ce:keyword><ce:text>Sturgeon</ce:text></ce:keyword><ce:keyword><ce:text>Fish</ce:text></ce:keyword><ce:keyword><ce:text>Neuropeptide</ce:text></ce:keyword><ce:keyword><ce:text>Brain peptide</ce:text></ce:keyword><ce:keyword><ce:text>Osteichthyes</ce:text></ce:keyword><ce:keyword><ce:text>Evolution</ce:text></ce:keyword></ce:keywords></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo><title>Mammalian gonadotropin-releasing hormone (GnRH) identified by primary structure in Russian sturgeon, Acipenser gueldenstaedti</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Mammalian gonadotropin-releasing hormone (GnRH) identified by primary structure in Russian sturgeon,</title></titleInfo><name type="personal"><namePart type="given">D.W.</namePart><namePart type="family">Lescheid</namePart><affiliation>Department of Biology, University of Victoria, Victoria, B.C., V8W 2Y2, Canada</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">J.F.F.</namePart><namePart type="family">Powell</namePart><affiliation>Department of Biology, University of Victoria, Victoria, B.C., V8W 2Y2, Canada</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">W.H.</namePart><namePart type="family">Fischer</namePart><affiliation>The Clayton Foundation Laboratories for Peptide Biology, The Salk Institute, La Jolla, CA 92037, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">M.</namePart><namePart type="family">Park</namePart><affiliation>The Clayton Foundation Laboratories for Peptide Biology, The Salk Institute, La Jolla, CA 92037, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">A.</namePart><namePart type="family">Craig</namePart><affiliation>The Clayton Foundation Laboratories for Peptide Biology, The Salk Institute, La Jolla, CA 92037, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">O.</namePart><namePart type="family">Bukovskaya</namePart><affiliation>Physiological Institute, St. Petersburg University, St. Petersburg 199034, Russian Federation</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">I.A.</namePart><namePart type="family">Barannikova</namePart><affiliation>Physiological Institute, St. Petersburg University, St. Petersburg 199034, Russian Federation</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">N.M.</namePart><namePart type="family">Sherwood</namePart><affiliation>Corresponding author.</affiliation><affiliation>Department of Biology, University of Victoria, Victoria, B.C., V8W 2Y2, Canada</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">1995</dateIssued><copyrightDate encoding="w3cdtf">1995</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">The mammalian form of gonadotropin-releasing hormone (GnRH) was purified from the brains of Russian sturgeon, Acipenser gueldenstaedti, using reversed-phase high pressure liquid chromatography (HPLC). The total concentration of mGnRH within these fish was 5.4 ng/brain. Small amounts of immunoreactive chicken GnRH-II like molecules were also detected but at insufficient quantities for purification. The primary structure of mGnRH was determined using automated Edman degradation. Because sequence data could not be obtained until after digestion by bovine pyroglutamyl aminopeptidase, it was determined that the amino-terminal residue was modified. Furthermore, mass spectrometric data and co-elution with synthetic mGnRH on HPLC confirmed that the carboxy-terminal residue was amidated. The amino acid sequence of sturgeon GnRH is pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2.</abstract><subject><genre>Keywords</genre><topic>Reproduction</topic><topic>Luteinizing hormone-releasing hormone</topic><topic>Sturgeon</topic><topic>Fish</topic><topic>Neuropeptide</topic><topic>Brain peptide</topic><topic>Osteichthyes</topic><topic>Evolution</topic></subject><relatedItem type="host"><titleInfo><title>Regulatory Peptides</title></titleInfo><titleInfo type="abbreviated"><title>REGPEP</title></titleInfo><genre type="journal">journal</genre><originInfo><dateIssued encoding="w3cdtf">19950214</dateIssued></originInfo><identifier type="ISSN">0167-0115</identifier><identifier type="PII">S0167-0115(00)X0023-7</identifier><part><date>19950214</date><detail type="volume"><number>55</number><caption>vol.</caption></detail><detail type="issue"><number>3</number><caption>no.</caption></detail><extent unit="issue pages"><start>219</start><end>341</end></extent><extent unit="pages"><start>299</start><end>309</end></extent></part></relatedItem><identifier type="istex">EF9B0369BC6ACADB6F0B0A548F4B69C0DEA68AEB</identifier><identifier type="DOI">10.1016/0167-0115(94)00118-H</identifier><identifier type="PII">0167-0115(94)00118-H</identifier><recordInfo><recordContentSource>ELSEVIER</recordContentSource></recordInfo></mods></metadata></istex></record>Pour manipuler ce document sous Unix (Dilib)
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