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Article: Purification and properties of chicken growth hormone and the development of a homologous radioimmunoassay

TitlePurification and properties of chicken growth hormone and the development of a homologous radioimmunoassay
Authors
Issue Date1984
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/ygcen
Citation
General And Comparative Endocrinology, 1984, v. 56 n. 3, p. 389-400 How to Cite?
AbstractHighly purified growth hormone (GH) has been isolated from pituitary glands of chicken (Gallus domesticus), and a specific homologous radioimmunoasssay (RIA) has also been developed. The purified chicken GH was active in the rat tibia bioassay and it gave a dose-dependent response which paralleled that of the bovine GH standard. High pressure liquid chromatography revealed that the purified chicken GH was homogenous. Chicken GH had an R(f) value of 0.2 in disc electrophoresis, and a MW of 26,000 from sodium dodecyl sulfategel elecltrophoresis. The isoelectric point was estimated to be 7.6 by gel isoelectric focusing. The amino acid composition of chicken GH was found to be similar to that of mammalian GH, and the NH 2-terminal amino acid was threonine. Partial sequencing (114 amino acids) of the chicken GH showed 79% homology with bovine GH. An antiserum was developed to the purified chicken GH in a rabbit, and it was used to develop a homologous RIA using 125I-labeled chicken GH as the ligand. The purified chicken GH was iodinated via the lactoperoxidase method to a specific activity of approximately 100 μCi/ug. Plasma from chickens, medium from incubation of pituitary glands, and homogenates of pituitary glands gave parallel dilution-response curves with the chicken GH standard. Mammalian GH, prolactin (PRL), follicle-stimulating hormone (FSH), and luteinizing hormone (LH) showed no cross-reaction with the 125I-labeled chicken GH. Purified turkey GH showed parallel dose response with the chicken GH, but purified turkey PRL did not cross-react. Chicken FSH and LH also showed no inhibition of binding. The minimum detectable concentration of the assay was 0.93 ng/tube, an the intraassay and interassay coefficients of variation were 9 and 16%, respectively. The specific binding of 125I-labeled chicken GH to a microsomal fraction isolated from chicken liver was identified, and the specific binding was generally low (1-4%). Turkey PRL, and chicken LH and FSH showed no inhibition of the 125I-labeled chicken GH hepatic binding and the ontogeny of the hepatic GH receptor binding site in male and female chickens was examined.
Persistent Identifierhttp://hdl.handle.net/10722/178428
ISSN
2015 Impact Factor: 2.667
2015 SCImago Journal Rankings: 1.245
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLeung, FCen_US
dc.contributor.authorTaylor, JEen_US
dc.contributor.authorSteelman, SLen_US
dc.date.accessioned2012-12-19T09:47:39Z-
dc.date.available2012-12-19T09:47:39Z-
dc.date.issued1984en_US
dc.identifier.citationGeneral And Comparative Endocrinology, 1984, v. 56 n. 3, p. 389-400en_US
dc.identifier.issn0016-6480en_US
dc.identifier.urihttp://hdl.handle.net/10722/178428-
dc.description.abstractHighly purified growth hormone (GH) has been isolated from pituitary glands of chicken (Gallus domesticus), and a specific homologous radioimmunoasssay (RIA) has also been developed. The purified chicken GH was active in the rat tibia bioassay and it gave a dose-dependent response which paralleled that of the bovine GH standard. High pressure liquid chromatography revealed that the purified chicken GH was homogenous. Chicken GH had an R(f) value of 0.2 in disc electrophoresis, and a MW of 26,000 from sodium dodecyl sulfategel elecltrophoresis. The isoelectric point was estimated to be 7.6 by gel isoelectric focusing. The amino acid composition of chicken GH was found to be similar to that of mammalian GH, and the NH 2-terminal amino acid was threonine. Partial sequencing (114 amino acids) of the chicken GH showed 79% homology with bovine GH. An antiserum was developed to the purified chicken GH in a rabbit, and it was used to develop a homologous RIA using 125I-labeled chicken GH as the ligand. The purified chicken GH was iodinated via the lactoperoxidase method to a specific activity of approximately 100 μCi/ug. Plasma from chickens, medium from incubation of pituitary glands, and homogenates of pituitary glands gave parallel dilution-response curves with the chicken GH standard. Mammalian GH, prolactin (PRL), follicle-stimulating hormone (FSH), and luteinizing hormone (LH) showed no cross-reaction with the 125I-labeled chicken GH. Purified turkey GH showed parallel dose response with the chicken GH, but purified turkey PRL did not cross-react. Chicken FSH and LH also showed no inhibition of binding. The minimum detectable concentration of the assay was 0.93 ng/tube, an the intraassay and interassay coefficients of variation were 9 and 16%, respectively. The specific binding of 125I-labeled chicken GH to a microsomal fraction isolated from chicken liver was identified, and the specific binding was generally low (1-4%). Turkey PRL, and chicken LH and FSH showed no inhibition of the 125I-labeled chicken GH hepatic binding and the ontogeny of the hepatic GH receptor binding site in male and female chickens was examined.en_US
dc.languageengen_US
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/ygcenen_US
dc.relation.ispartofGeneral and Comparative Endocrinologyen_US
dc.subject.meshAgingen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAnimalsen_US
dc.subject.meshBiological Assayen_US
dc.subject.meshCattleen_US
dc.subject.meshChickensen_US
dc.subject.meshChromatography, High Pressure Liquiden_US
dc.subject.meshFemaleen_US
dc.subject.meshGrowth Hormone - Analysis - Metabolism - Pharmacologyen_US
dc.subject.meshHumansen_US
dc.subject.meshMaleen_US
dc.subject.meshMicrosomes, Liver - Metabolismen_US
dc.subject.meshMolecular Weighten_US
dc.subject.meshPituitary Gland - Analysisen_US
dc.subject.meshRadioimmunoassayen_US
dc.subject.meshRatsen_US
dc.subject.meshReceptors, Cell Surface - Metabolismen_US
dc.subject.meshReceptors, Somatotropinen_US
dc.subject.meshSpecies Specificityen_US
dc.subject.meshThyrotropin-Releasing Hormone - Pharmacologyen_US
dc.subject.meshTibia - Drug Effectsen_US
dc.titlePurification and properties of chicken growth hormone and the development of a homologous radioimmunoassayen_US
dc.typeArticleen_US
dc.identifier.emailLeung, FC: fcleung@hkucc.hku.hken_US
dc.identifier.authorityLeung, FC=rp00731en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/0016-6480(84)90081-9-
dc.identifier.pmid6096203-
dc.identifier.scopuseid_2-s2.0-0021713370en_US
dc.identifier.volume56en_US
dc.identifier.issue3en_US
dc.identifier.spage389en_US
dc.identifier.epage400en_US
dc.identifier.isiWOS:A1984TV25800006-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridLeung, FC=7103078633en_US
dc.identifier.scopusauthoridTaylor, JE=7405405625en_US
dc.identifier.scopusauthoridSteelman, SL=6701781251en_US

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