title: The primary structure of the hemoglobin of the Indian false vampire (Megaderma lyra, Microchiroptera).
abstract: The hemoglobin of the Indian false vampire Megaderma lyra contains only one component. In this paper, 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 prolyl-peptides obtained by acid hydrolysis of the Asp-Pro bond in the alpha- and beta-chains. The alpha-chains show 23 and the beta-chains 20 exchanges compared with the human alpha- and beta-chains, respectively. In the alpha-chains, three exchanges involved alpha 1/beta 1 contacts. In the beta-chains one heme-and three alpha 1/beta 1 contacts are exchanged. The functional and systematic aspects of these replacements are discussed.
authors.affiliation: Max-Planck-Institut für Biochemie, Abteilung Proteinchemie, Martinsried bei München.
authors.forename: J G
authors.initials: JG
authors.lastname: Sgouros
authors.forename: T
authors.initials: T
authors.lastname: Kleinschmidt
authors.forename: G
authors.initials: G
authors.lastname: Braunitzer
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002685:Chiroptera / Q000097:blood*; D005914:Globins / Q000032:analysis; D006454:Hemoglobins / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D011487:Protein Conformation
chemical_list: D006454:Hemoglobins; D010446:Peptide Fragments; D005914:Globins