The Primary Structure of the Hemoglobin from the Tomb Bat (Taphozous georgianus, Microchiroptera)

The primary structures of the α- and β-chains of the single hemoglobin component from the tomb bat (Taphozous georgianus, Microchiroptera) are presented. After chain separation by reversed-phase HPLC the sequences could be determined by automatic gas and liquid phase Edman degradation of the chains and their tryptic peptides. The α- and β-chains differ from human hemoglobin by 14 and 18 replacements, respectively. Compared to the total number of amino-acid exchanges, the exchange rate in the interhelical regions of the α-chains is surprisingly high (25%). It seems unlikely that substitutions at contact positions affect the oxygen binding properties of the hemoglobin.