{"id":{"repo_id":"cape-town","oai_identifier":"oai:open.uct.ac.za:11427/27260"},"canonical_url":"https://search.dev.ndltd.org/etd/cape-town/oai:open.uct.ac.za:11427/27260","repository":{"repo_id":"cape-town","name":"University of Cape Town","base_url":"https://open.uct.ac.za/oai/request"},"display":{"title":"Structure and biological activity of avian hypothalamic luteinizing hormone-releasing hormone","abstract":"In 1971 Schally and co-workers (Schally et al., 1971) isolated gonadotropin-releasing hormone (now called luteinizing hormone-releasing hormone (LH-RH)) from sheep hypothalami and established that the hormone was a decapeptide with the amino acid sequence: pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH₂. The peptide was subsequently synthesised (Matsuo et al., 1971b) and shown to stimulate the release of gonadotropins (luteinizing hormone and follicle-stimulating hormone) in a wide range of mammalian species (Schally et al., 1973, 1976). With the exception of amphibians, nonmammalian vertebrates have a poor gonadotropin response to synthetic mammalian LH-RH (for reviews, see Ball, 1981; Jackson, 1981; King and Millar, 1981a). Since there is considerable molecular heterogeneity in the related neurohypophysial nonapeptide hormones (oxytocin-vasopressin) amongst vertebrates (Acher et al., 1972), we postulated that differences might exist in the structure of hypothalamic LH-RH in different vertebrate classes, Utilising a combination of regionspecific antisera and chromatographic techniques, we established that amphibian hypothalamic LH-RH is identical to the mammalian peptide while avian, reptilian, and piscine hypothalamic LH-RHs differ structurally in the region Gly⁶-Leu⁷-Arg⁸ (King and Millar, 1979a, 1980), We have now conducted further studies on avian hypothalamic LH-RH, which indicate that the arginine residue in position eight of mammalian LH-RH is substituted by glutamine in this vertebrate class. Purification of LH-RH from chicken hypothalami and determination of the amino acid composition have confirmed that the structure of avian LH-RH is: pGlu-His-Trp-Ser-Tyr-Gly-Leu-Gln-Pro-Gly-NH₂.","abstract_html":"In 1971 Schally and co-workers (Schally et al., 1971) isolated gonadotropin-releasing hormone (now called luteinizing hormone-releasing hormone (LH-RH)) from sheep hypothalami and established that the hormone was a decapeptide with the amino acid sequence: pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH₂. The peptide was subsequently synthesised (Matsuo et al., 1971b) and shown to stimulate the release of gonadotropins (luteinizing hormone and follicle-stimulating hormone) in a wide range of mammalian species (Schally et al., 1973, 1976). With the exception of amphibians, nonmammalian vertebrates have a poor gonadotropin response to synthetic mammalian LH-RH (for reviews, see Ball, 1981; Jackson, 1981; King and Millar, 1981a). Since there is considerable molecular heterogeneity in the related neurohypophysial nonapeptide hormones (oxytocin-vasopressin) amongst vertebrates (Acher et al., 1972), we postulated that differences might exist in the structure of hypothalamic LH-RH in different vertebrate classes, Utilising a combination of regionspecific antisera and chromatographic techniques, we established that amphibian hypothalamic LH-RH is identical to the mammalian peptide while avian, reptilian, and piscine hypothalamic LH-RHs differ structurally in the region Gly⁶-Leu⁷-Arg⁸ (King and Millar, 1979a, 1980), We have now conducted further studies on avian hypothalamic LH-RH, which indicate that the arginine residue in position eight of mammalian LH-RH is substituted by glutamine in this vertebrate class. Purification of LH-RH from chicken hypothalami and determination of the amino acid composition have confirmed that the structure of avian LH-RH is: pGlu-His-Trp-Ser-Tyr-Gly-Leu-Gln-Pro-Gly-NH₂.","abstract_has_math":false,"creators":["King, Judy A"],"institution":"Division of Chemical Pathology","degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":["Millar, Robert P"],"committee_chairs":[],"committee_members":[],"year":1982,"date_issued":"1982","date_published":"1982","updated_at":"2026-07-22T22:23:24Z","subjects":[],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/11427/27260","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Millar, Robert P"]},{"key":"dc:creator","label":"Author","values":["King, Judy A"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2018-02-05T12:35:52Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2018-02-05T12:35:52Z"]},{"key":"dc:date.issued","label":"Date","values":["1982"]},{"key":"dc:publisher.department","label":"Dc Publisher Department","values":["Division of Chemical Pathology"]},{"key":"dc:publisher.institution","label":"Dc Publisher Institution","values":["University of Cape Town"]},{"key":"dc:type","label":"Dc Type","values":["Doctoral Thesis"]},{"key":"dc:type.qualificationlevel","label":"Dc Type Qualificationlevel","values":["Doctoral"]},{"key":"dc:type.qualificationname","label":"Dc Type Qualificationname","values":["PhD"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language.iso","label":"Language (ISO)","values":["eng"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["http://hdl.handle.net/11427/27260"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["In 1971 Schally and co-workers (Schally et al., 1971) isolated gonadotropin-releasing hormone (now called luteinizing hormone-releasing hormone (LH-RH)) from sheep hypothalami and established that the hormone was a decapeptide with the amino acid sequence: pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH₂. The peptide was subsequently synthesised (Matsuo et al., 1971b) and shown to stimulate the release of gonadotropins (luteinizing hormone and follicle-stimulating hormone) in a wide range of mammalian species (Schally et al., 1973, 1976). With the exception of amphibians, nonmammalian vertebrates have a poor gonadotropin response to synthetic mammalian LH-RH (for reviews, see Ball, 1981; Jackson, 1981; King and Millar, 1981a). Since there is considerable molecular heterogeneity in the related neurohypophysial nonapeptide hormones (oxytocin-vasopressin) amongst vertebrates (Acher et al., 1972), we postulated that differences might exist in the structure of hypothalamic LH-RH in different vertebrate classes, Utilising a combination of regionspecific antisera and chromatographic techniques, we established that amphibian hypothalamic LH-RH is identical to the mammalian peptide while avian, reptilian, and piscine hypothalamic LH-RHs differ structurally in the region Gly⁶-Leu⁷-Arg⁸ (King and Millar, 1979a, 1980), We have now conducted further studies on avian hypothalamic LH-RH, which indicate that the arginine residue in position eight of mammalian LH-RH is substituted by glutamine in this vertebrate class. Purification of LH-RH from chicken hypothalami and determination of the amino acid composition have confirmed that the structure of avian LH-RH is: pGlu-His-Trp-Ser-Tyr-Gly-Leu-Gln-Pro-Gly-NH₂."]},{"key":"dc:title","label":"Title","values":["Structure and biological activity of avian hypothalamic luteinizing hormone-releasing hormone"]}]}],"canonical_facts":{"dc:contributor.advisor":["Millar, Robert P"],"dc:creator":["King, Judy A"],"dc:date.accessioned":["2018-02-05T12:35:52Z"],"dc:date.available":["2018-02-05T12:35:52Z"],"dc:date.issued":["1982"],"dc:description.abstract":["In 1971 Schally and co-workers (Schally et al., 1971) isolated gonadotropin-releasing hormone (now called luteinizing hormone-releasing hormone (LH-RH)) from sheep hypothalami and established that the hormone was a decapeptide with the amino acid sequence: pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH₂. The peptide was subsequently synthesised (Matsuo et al., 1971b) and shown to stimulate the release of gonadotropins (luteinizing hormone and follicle-stimulating hormone) in a wide range of mammalian species (Schally et al., 1973, 1976). With the exception of amphibians, nonmammalian vertebrates have a poor gonadotropin response to synthetic mammalian LH-RH (for reviews, see Ball, 1981; Jackson, 1981; King and Millar, 1981a). Since there is considerable molecular heterogeneity in the related neurohypophysial nonapeptide hormones (oxytocin-vasopressin) amongst vertebrates (Acher et al., 1972), we postulated that differences might exist in the structure of hypothalamic LH-RH in different vertebrate classes, Utilising a combination of regionspecific antisera and chromatographic techniques, we established that amphibian hypothalamic LH-RH is identical to the mammalian peptide while avian, reptilian, and piscine hypothalamic LH-RHs differ structurally in the region Gly⁶-Leu⁷-Arg⁸ (King and Millar, 1979a, 1980), We have now conducted further studies on avian hypothalamic LH-RH, which indicate that the arginine residue in position eight of mammalian LH-RH is substituted by glutamine in this vertebrate class. Purification of LH-RH from chicken hypothalami and determination of the amino acid composition have confirmed that the structure of avian LH-RH is: pGlu-His-Trp-Ser-Tyr-Gly-Leu-Gln-Pro-Gly-NH₂."],"dc:identifier.uri":["http://hdl.handle.net/11427/27260"],"dc:language.iso":["eng"],"dc:publisher.department":["Division of Chemical Pathology"],"dc:publisher.institution":["University of Cape Town"],"dc:title":["Structure and biological activity of avian hypothalamic luteinizing hormone-releasing hormone"],"dc:type":["Doctoral Thesis"],"dc:type.qualificationlevel":["Doctoral"],"dc:type.qualificationname":["PhD"]},"updated_at":"2026-07-22T22:23:24Z"}