The Primary Structure of a Mouse-Eared Bat(Myotis velifer,Chiroptera) Hemoglobin

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Abstract
The hemoglobin of the Mouse-Eared Bat Myotis velifer consists of one component. We present the primary structures of the .alpha.- and .beta.-globin chains which have been separated by chromatography on carboxymethyl-cellulose CM-52. The sequences have been determined by Edman-degradation with the film technic or the gas phase method, using the native chains and the typtic peptides, as well as the C-terminal prolyl-peptides obtained by acid hydrolysis of the Asp-Pro-bonds. Compared to the corresponding human chains we found only 13 substitutions in the .alpha.-chains, but 27 in the .beta.-chains. The amino-acid residues substituted in the .alpha.-chains are not involved in any contacts, whereas in the .beta.-chains, one exchange involves a heme contact, three .alpha.1/.beta.1- and one .alpha.1/.beta.2-contacts, the latter [.beta.43(CD2)-Glu .fwdarw. Thr] brings for the first time threonine in this position of the .beta.-chains. Comparison with the Egyptian Fruit Bat (Rousettus aegyptiacus) shows 12 and 25 substitutions in the .alpha.- and .beta.-chains, respectively, suggesting a large phylogenetic distance between Micro- and Megachiroptera. We consider this primary structure as a contribution towards solving the problem of the origin of bats and their relation to primates.