The primary structure of the hemoglobin from the grey-headed flying fox (Pteropus poliocephalus) and the black flying fox (P. alecto, Megachiroptera).

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 11 and two beta-chains at a ratio of 41 were detected. The hemoglobin of P. poliocephalus comprises one alpha-chain and two beta-chains, the latter at a ratio of 11. 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.