Structure and biological activity of avian hypothalamic luteinizing hormone-releasing hormone

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dc.contributor.advisorMillar, Robert Pen_ZA
dc.contributor.authorKing, Judy Aen_ZA
dc.date.accessioned2018-02-05T12:35:52Z
dc.date.available2018-02-05T12:35:52Z
dc.date.issued1982en_ZA
dc.description.abstractIn 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.en_ZA
dc.identifier.apacitationKing, J. A. (1982). <i>Structure and biological activity of avian hypothalamic luteinizing hormone-releasing hormone</i>. (Thesis). University of Cape Town ,Faculty of Health Sciences ,Division of Chemical Pathology. Retrieved from http://hdl.handle.net/11427/27260en_ZA
dc.identifier.chicagocitationKing, Judy A. <i>"Structure and biological activity of avian hypothalamic luteinizing hormone-releasing hormone."</i> Thesis., University of Cape Town ,Faculty of Health Sciences ,Division of Chemical Pathology, 1982. http://hdl.handle.net/11427/27260en_ZA
dc.identifier.citationKing, J. 1982. Structure and biological activity of avian hypothalamic luteinizing hormone-releasing hormone. University of Cape Town.en_ZA
dc.identifier.ris TY - Thesis / Dissertation AU - King, Judy A AB - 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. DA - 1982 DB - OpenUCT DP - University of Cape Town LK - https://open.uct.ac.za PB - University of Cape Town PY - 1982 T1 - Structure and biological activity of avian hypothalamic luteinizing hormone-releasing hormone TI - Structure and biological activity of avian hypothalamic luteinizing hormone-releasing hormone UR - http://hdl.handle.net/11427/27260 ER - en_ZA
dc.identifier.urihttp://hdl.handle.net/11427/27260
dc.identifier.vancouvercitationKing JA. Structure and biological activity of avian hypothalamic luteinizing hormone-releasing hormone. [Thesis]. University of Cape Town ,Faculty of Health Sciences ,Division of Chemical Pathology, 1982 [cited yyyy month dd]. Available from: http://hdl.handle.net/11427/27260en_ZA
dc.language.isoengen_ZA
dc.publisher.departmentDivision of Chemical Pathologyen_ZA
dc.publisher.facultyFaculty of Health Sciencesen_ZA
dc.publisher.institutionUniversity of Cape Town
dc.subject.otherHypothalamic hormonesen_ZA
dc.subject.otherGonadorelinen_ZA
dc.subject.otherChickensen_ZA
dc.titleStructure and biological activity of avian hypothalamic luteinizing hormone-releasing hormoneen_ZA
dc.typeDoctoral Thesis
dc.type.qualificationlevelDoctoral
dc.type.qualificationnamePhDen_ZA
uct.type.filetypeText
uct.type.filetypeImage
uct.type.publicationResearchen_ZA
uct.type.resourceThesisen_ZA
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