{"title":"Amino acid sequence of alpha- and beta-polypeptide chains of turkey (Meleagris gallopavo) hemoglobin.","authors":"Y Eguchi, T Ikehara, S Kayo, T Eguchi, H Takei","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Two hemoglobin components are recognized in erythrocytes of the adult turkey (Meleagris gallopavo). We determined the amino acid sequences of turkey alpha A-, alpha D- and beta-globin from intact globin chains and chemical cleavage fragments. The sequences are highly similar to the hemoglobin of the Phasianidae, chicken, Japanese quail and pheasant. Turkey and pheasant beta-globin are identical. The amino acid sequence of turkey alpha A-globin differs by only one residue from chicken alpha A-globin. Phylogeny trees from alpha A-, alpha D- and beta-globin were constructed by the neighbor-joining method. Although the trees generated from alpha A- and beta-globin were similar, that from turkey alpha D-globin differed.</p>","PeriodicalId":8963,"journal":{"name":"Biological chemistry Hoppe-Seyler","volume":"376 7","pages":"437-40"},"PeriodicalIF":0.0000,"publicationDate":"1995-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biological chemistry Hoppe-Seyler","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
Two hemoglobin components are recognized in erythrocytes of the adult turkey (Meleagris gallopavo). We determined the amino acid sequences of turkey alpha A-, alpha D- and beta-globin from intact globin chains and chemical cleavage fragments. The sequences are highly similar to the hemoglobin of the Phasianidae, chicken, Japanese quail and pheasant. Turkey and pheasant beta-globin are identical. The amino acid sequence of turkey alpha A-globin differs by only one residue from chicken alpha A-globin. Phylogeny trees from alpha A-, alpha D- and beta-globin were constructed by the neighbor-joining method. Although the trees generated from alpha A- and beta-globin were similar, that from turkey alpha D-globin differed.