Mammalian gonadotropin-releasing hormone (GnRH) identified by primary structure in Russian sturgeon, Acipenser gueldenstaedti
Identifieur interne : 001A19 ( Main/Curation ); précédent : 001A18; suivant : 001A20Mammalian gonadotropin-releasing hormone (GnRH) identified by primary structure in Russian sturgeon, Acipenser gueldenstaedti
Auteurs : D. W. Lescheid [Canada] ; J. F. F. Powell [Canada] ; W. H. Fischer [États-Unis] ; M. Park [États-Unis] ; A. Craig [États-Unis] ; O. Bukovskaya [Russie] ; I. A. Barannikova [Russie] ; N. M. Sherwood [Canada]Source :
- Regulatory Peptides [ 0167-0115 ] ; 1995.
Descripteurs français
- Pascal (Inist)
English descriptors
- KwdEn :
- Amino Acid Sequence, Aminoacid sequence, Animals, Biological evolution, Brain Chemistry, Chromatography, High Pressure Liquid, Female, Fishes, Gonadotropin RH, Gonadotropin-Releasing Hormone (analysis), Gonadotropin-Releasing Hormone (chemistry), Male, Mass Spectrometry, Molecular Sequence Data, Purification, Sequence Analysis.
- MESH :
- chemical , analysis : Gonadotropin-Releasing Hormone.
- chemical , chemistry : Gonadotropin-Releasing Hormone.
- Amino Acid Sequence, Animals, Brain Chemistry, Chromatography, High Pressure Liquid, Female, Fishes, Male, Mass Spectrometry, Molecular Sequence Data, Sequence Analysis.
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
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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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<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-NH<sub>2</sub>
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<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>
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<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>
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<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>
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<wicri:regionArea>Department of Biology, University of Victoria, Victoria, B.C., V8W 2Y2</wicri:regionArea>
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<author><name sortKey="Fischer, W H" sort="Fischer, W H" uniqKey="Fischer W" first="W. H." last="Fischer">W. H. Fischer</name>
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<wicri:regionArea>The Clayton Foundation Laboratories for Peptide Biology, The Salk Institute, La Jolla, CA 92037</wicri:regionArea>
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<author><name sortKey="Park, M" sort="Park, M" uniqKey="Park M" first="M." last="Park">M. Park</name>
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<wicri:regionArea>The Clayton Foundation Laboratories for Peptide Biology, The Salk Institute, La Jolla, CA 92037</wicri:regionArea>
<placeName><region type="state">Californie</region>
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<author><name sortKey="Craig, A" sort="Craig, A" uniqKey="Craig A" first="A." last="Craig">A. Craig</name>
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<wicri:regionArea>The Clayton Foundation Laboratories for Peptide Biology, The Salk Institute, La Jolla, CA 92037</wicri:regionArea>
<placeName><region type="state">Californie</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="Bukovskaya, O" sort="Bukovskaya, O" uniqKey="Bukovskaya O" first="O." last="Bukovskaya">O. Bukovskaya</name>
<affiliation wicri:level="1"><country xml:lang="fr">Russie</country>
<wicri:regionArea>Physiological Institute, St. Petersburg University, St. Petersburg 199034</wicri:regionArea>
<wicri:noRegion>St. Petersburg 199034</wicri:noRegion>
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<author><name sortKey="Barannikova, I A" sort="Barannikova, I A" uniqKey="Barannikova I" first="I. A." last="Barannikova">I. A. Barannikova</name>
<affiliation wicri:level="1"><country xml:lang="fr">Russie</country>
<wicri:regionArea>Physiological Institute, St. Petersburg University, St. Petersburg 199034</wicri:regionArea>
<wicri:noRegion>St. Petersburg 199034</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Sherwood, N M" sort="Sherwood, N M" uniqKey="Sherwood N" first="N. M." last="Sherwood">N. M. Sherwood</name>
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<affiliation wicri:level="1"><country xml:lang="fr">Canada</country>
<wicri:regionArea>Department of Biology, University of Victoria, Victoria, B.C., V8W 2Y2</wicri:regionArea>
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<series><title level="j">Regulatory Peptides</title>
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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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<author><name sortKey="Powell, J F" sort="Powell, J F" uniqKey="Powell J" first="J F" last="Powell">J F Powell</name>
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<author><name sortKey="Fischer, W H" sort="Fischer, W H" uniqKey="Fischer W" first="W H" last="Fischer">W H Fischer</name>
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<author><name sortKey="Park, M" sort="Park, M" uniqKey="Park M" first="M" last="Park">M. Park</name>
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<author><name sortKey="Craig, A" sort="Craig, A" uniqKey="Craig A" first="A" last="Craig">A. Craig</name>
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<author><name sortKey="Bukovskaya, O" sort="Bukovskaya, O" uniqKey="Bukovskaya O" first="O" last="Bukovskaya">O. Bukovskaya</name>
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<author><name sortKey="Barannikova, I A" sort="Barannikova, I A" uniqKey="Barannikova I" first="I A" last="Barannikova">I A Barannikova</name>
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<author><name sortKey="Fischer, W H" sort="Fischer, W H" uniqKey="Fischer W" first="W H" last="Fischer">W H Fischer</name>
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<author><name sortKey="Park, M" sort="Park, M" uniqKey="Park M" first="M" last="Park">M. Park</name>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Animals</term>
<term>Brain Chemistry</term>
<term>Chromatography, High Pressure Liquid</term>
<term>Female</term>
<term>Fishes</term>
<term>Gonadotropin-Releasing Hormone (analysis)</term>
<term>Gonadotropin-Releasing Hormone (chemistry)</term>
<term>Male</term>
<term>Mass Spectrometry</term>
<term>Molecular Sequence Data</term>
<term>Sequence Analysis</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Gonadotropin-Releasing Hormone</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Gonadotropin-Releasing Hormone</term>
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<term>Animals</term>
<term>Brain Chemistry</term>
<term>Chromatography, High Pressure Liquid</term>
<term>Female</term>
<term>Fishes</term>
<term>Male</term>
<term>Mass Spectrometry</term>
<term>Molecular Sequence Data</term>
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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 amino-peptidase, 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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