The primary structure of the hemoglobin of the Indian false vampire (Megaderma lyra, Microchiroptera).
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.
Sgouros
J G
JG
Max-Planck-Institut für Biochemie, Abteilung Proteinchemie, Martinsried bei München.
Kleinschmidt
T
T
Braunitzer
G
G
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
D006454:Hemoglobins; D010446:Peptide Fragments; D005914:Globins