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Biol Chem Hoppe Seyler. 1992 Sep;373(9):937-42.

The primary structure of the hemoglobin from the tomb bat (Taphozous georgianus, Microchiroptera).

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Max-Planck-Institut für Biochemie, Abteilung Proteinchemie, Martinsried bei München.


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.

[Indexed for MEDLINE]

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