Die Primärstruktur des Hämoglobins vom Ägyptischen Flughund (Rousettus aegyptiacus,Chiroptera)

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Abstract
The Hb of the Egyptian fruit bat (R. aegyptiacus) has only 1 component. The .alpha. and .beta. chains were separated by chromatography on CM-52 cellulose. The complete primary structures of both chains were established by automatic Edman degradation of the chains and the tryptic peptides. The alignment was done by homology with .alpha. and .beta. chains of adult human Hb. A comparison of these 2 Hb shows an exchange of 14 amino acid residues in the .alpha. chains and of 19 in the .beta. chains. These numbers are very low, considering the long phylogenetic distance between primates and megachiroptera. In the surroundings of the heme, 1 substitution was found in each chain. In the .alpha.1.beta.1-subunit interface, 1 and 2 residues are exchanged, respectively, in the .alpha. and .beta. chains. The primary structure points to a normal O2 affinity of the bat Hb, which was also found by Jurgens et al.

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