Abstract
The complete primary structure of the two hemoglobin components of the domestic cat (Felis catus) is presented. The major component (A) accounts for 60-70% whereas the minor component (B) constitutes 30-40% of the total hemoglobin. Separation of the polypeptides was carried out in buffers containing 8M urea on CM-Cellulose. The sequence was studied by Edman degradation of tryptic and cyanogen bromide cleavage products in a liquid phase sequencer. The sequence is compared for homology with human hemoglobin. The beta-chain of the minor components (beta B) has a blocked N-terminal residue identified as acetylserine whereas that of the major component (beta A) is free glycine. The two hemoglobins have identical alpha-chains and differ with respect to their beta-chains at the following positions (beta B/beta A): beta NA1 Ac-Ser/Gly, beta A1 Ser/Thr, beta H17 Ser/Asn and beta HC1 Arg/Lys. The structural and functional aspects of these exchanges are discussed.
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