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  • Title: The primary structure of the hemoglobin from the grey-headed flying fox (Pteropus poliocephalus) and the black flying fox (P. alecto, Megachiroptera).
    Author: Kleinschmidt T, Sgouros JG, Pettigrew JD, Braunitzer G.
    Journal: Biol Chem Hoppe Seyler; 1988 Sep; 369(9):975-84. PubMed ID: 3228493.
    Abstract:
    The primary structures of the hemoglobins of two Flying Foxes of the genus Pteropus are presented. Both comprise two components: in P. alecto hemoglobin two alpha-chains at a ratio of 1:1 and two beta-chains at a ratio of 4:1 were detected. The hemoglobin of P. poliocephalus comprises one alpha-chain and two beta-chains, the latter at a ratio of 1:1. 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. Compared with human hemoglobin, the alpha-chains of P. alecto and P. poliocephalus show 18 and 19 exchanges, respectively, whereas in the beta-chains 16/17 substitutions are found in both cases. In the alpha-chains of P. alecto, one exchange involves an alpha 1/beta 1-contact. In the beta-chains of both species one heme-, one alpha 1/beta 2- and two alpha 1/beta 1-contacts are exchanged. The relevant side chains are the same in both species. The functional and systematic aspects of these findings are discussed.
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