{"title":"Purification and partial characterization of isoforms of luteinizing hormone from the chicken pituitary gland.","authors":"K A Krishnan, J A Proudman, J M Bahr","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Isoforms of chicken luteinizing hormone (cLH) were isolated from chicken pituitaries by differential extraction, sequential chromatography on HPLC cation- and anion-exchange columns, and gel-filtration chromatography. Three purified isoforms of the cLH had high biological potency in the chicken granulosa cell LH bioassay (4.21-7.4 x NIH-LH-S1 U/mg). One cLH isoform without detectable biological activity showed substantial immunological activity in a homologous cLH radioimmunoassay. The cLH isoforms contained negligible follicle-stimulating hormone activity, but some contained thyroid-stimulating hormone activity. The apparent molecular weight of cLH was 37,000 Da, and the holoprotein consisted of subunits with a molecular weight of approximately 17,000 Da.</p>","PeriodicalId":79327,"journal":{"name":"Comparative biochemistry and physiology. Biochemistry and molecular biology","volume":"108 2","pages":"253-64"},"PeriodicalIF":0.0000,"publicationDate":"1994-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Comparative biochemistry and physiology. Biochemistry and molecular biology","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
Abstract
Isoforms of chicken luteinizing hormone (cLH) were isolated from chicken pituitaries by differential extraction, sequential chromatography on HPLC cation- and anion-exchange columns, and gel-filtration chromatography. Three purified isoforms of the cLH had high biological potency in the chicken granulosa cell LH bioassay (4.21-7.4 x NIH-LH-S1 U/mg). One cLH isoform without detectable biological activity showed substantial immunological activity in a homologous cLH radioimmunoassay. The cLH isoforms contained negligible follicle-stimulating hormone activity, but some contained thyroid-stimulating hormone activity. The apparent molecular weight of cLH was 37,000 Da, and the holoprotein consisted of subunits with a molecular weight of approximately 17,000 Da.
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