Singer G A, Kleinschmidt T, Pettigrew J D, Braunitzer G
Max-Planck-Institut für Biochemie, Abteilung Proteinchemie, Martinsried bei München.
Biol Chem Hoppe Seyler. 1992 Sep;373(9):937-42. doi: 10.1515/bchm3.1992.373.2.937.
The primary structures of the alpha- and beta-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 alpha- and beta-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 alpha-chains is surprisingly high (25%). It seems unlikely that substitutions at contact positions affect the oxygen binding properties of the hemoglobin.
