Avian luteinizing hormone-releasing hormone (LH-RH) has been isolated from 249,000 chicken hypothalami and shown to differ structurally from mammalian hypothalamic LH-RH. Purification was achieved by acetic acid extraction, anti-LH-RH affinity chromatography, and cation exchange and reverse phase high performance liquid chromatography. The isolated peptide eluted as a single peak on reverse phase high performance liquid chromatography. Acid hydrolysis of the peptide yielded integral molar ratios of amino acids and a composition identical with that of mammalian decapeptide LH-RH, except for the presence of an additional glutamic acid residue and the absence of arginine. The isoelectric point of chicken LH-RH (7.3) is consistent with the glutamic acid representing a glutamine residue. We therefore synthesized [Gln8]LH-RH and established that it has chromatographic properties identical with natural chicken LH-RH. These studies indicate that the structure of chicken hypothalamic LH-RH is: pGlu-His-Trp-Ser-Tyr-Gly-Leu-Gln-Pro-Gly-NH2.
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|---|---|---|---|
| http://purl.uniprot.org/cit... | rdf:type | uniprot:Journal_Citation | lld:uniprot |
| http://purl.uniprot.org/cit... | rdfs:comment | Avian luteinizing hormone-releasing hormone (LH-RH) has been isolated from 249,000 chicken hypothalami and shown to differ structurally from mammalian hypothalamic LH-RH. Purification was achieved by acetic acid extraction, anti-LH-RH affinity chromatography, and cation exchange and reverse phase high performance liquid chromatography. The isolated peptide eluted as a single peak on reverse phase high performance liquid chromatography. Acid hydrolysis of the peptide yielded integral molar ratios of amino acids and a composition identical with that of mammalian decapeptide LH-RH, except for the presence of an additional glutamic acid residue and the absence of arginine. The isoelectric point of chicken LH-RH (7.3) is consistent with the glutamic acid representing a glutamine residue. We therefore synthesized [Gln8]LH-RH and established that it has chromatographic properties identical with natural chicken LH-RH. These studies indicate that the structure of chicken hypothalamic LH-RH is: pGlu-His-Trp-Ser-Tyr-Gly-Leu-Gln-Pro-Gly-NH2. | lld:uniprot |
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| http://purl.uniprot.org/cit... | skos:exactMatch | http://purl.uniprot.org/pub... | lld:uniprot |
| http://purl.uniprot.org/cit... | uniprot:name | J. Biol. Chem. | lld:uniprot |
| http://purl.uniprot.org/cit... | uniprot:author | Millar R.P. | lld:uniprot |
| http://purl.uniprot.org/cit... | uniprot:author | King J.A. | lld:uniprot |
| http://purl.uniprot.org/cit... | uniprot:date | 1982 | lld:uniprot |
| http://purl.uniprot.org/cit... | uniprot:pages | 10729-10732 | lld:uniprot |
| http://purl.uniprot.org/cit... | uniprot:title | Structure of chicken hypothalamic luteinizing hormone-releasing hormone. II. Isolation and characterization. | lld:uniprot |
| http://purl.uniprot.org/cit... | uniprot:volume | 257 | lld:uniprot |
| uniprot-protein:P37042 | uniprot:citation | http://purl.uniprot.org/cit... | lld:uniprot |
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