The Primary Structure of the Pallid Bat(Antrozous pallidus,Chiroptera) Hämoglobin

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Abstract
The complete primary structure of the hemoglobin from the Pallid Bat (Antrozous pallidus, Microchiroptera) is presented. This hemoglobin consists of two components with identical amino-acid sequences, differing, however, in the N-terminus which is formylated in 12.5% of the .beta.-chains. The .alpha.- and .beta.-chains were separated by reversed phase high performance liquid chromatography. The sequences of both chains were established by automatic Edman degradation with the film technique or gas phase method using the native chains and the tryptic peptides. The formylation of a part of the N-terminal peptide of the .beta.-chains was determined by mass spectrometric examination. Compared to the corresponding human chains we found 14 substitutions in the .alpha.-chains and 21 in the .beta.-chains. One substitution in the .alpha.-chains and three in the .beta.-chains are involved in .alpha.1/.beta.1-contacts. Among these the exchange .beta.123(H1)Thr .fwdarw. Cys is unusual because cysteine was so far not found in this position of mammalian .beta.-chains. Compared to the hemoglobin of Myotis velifer, another representative of the family Vespertilionidae, 5 residues are replaced in the .alpha.-chains and 18 in the .beta.-chains.