title: The primary structure of the hemoglobin of an Indian flying fox (Cynopterus sphinx, Megachiroptera).
abstract: The hemoglobin of the Indian flying fox Cynopterus sphinx contains only one component. In this work, we are presenting its primary structure. The globin chains were separated by high-performance liquid chromatography and the sequences determined by automatic liquid and gas-phase Edman degradation of the chains and their tryptic peptides, as well as of the peptide obtained by acid hydrolysis of the Asp-Pro bond in the beta-chains. The alpha-chains show 14 and the beta-chains 19 exchanges compared with the human alpha- and beta-chains, respectively. In the alpha-chains one amino-acid exchange involves an alpha 1/beta 1 contact. In the beta-chains one heme contact, three alpha 1/beta 1- and one alpha 1/beta 2-contacts are exchanged. The functional and evolutionary aspects of these findings are discussed.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002685:Chiroptera / Q000097:blood*; D002851:Chromatography, High Pressure Liquid; D004912:Erythrocytes / Q000032:analysis*; D005914:Globins / Q000032:analysis*; D006454:Hemoglobins / Q000032:analysis*; D010446:Peptide Fragments / Q000032:analysis
chemical_list: D006454:Hemoglobins; D010446:Peptide Fragments; D005914:Globins