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.
Url:
DOI: 10.1016/0167-0115(94)00118-H
Links to Exploration step
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<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>
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<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>
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<mods version="3.6"><titleInfo><title>Mammalian gonadotropin-releasing hormone (GnRH) identified by primary structure in Russian sturgeon, Acipenser gueldenstaedti</title>
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<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>
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<dateIssued encoding="w3cdtf">1995</dateIssued>
<copyrightDate encoding="w3cdtf">1995</copyrightDate>
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<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>
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