Carnivora: Primary Structure of the Hemoglobins from Ratel(Mellivora Capensis)

Abstract
The erythrocytes of adult ratel contain two hemoglobin components, with two .alpha.- and one .beta.-chains. In this paper, their complete amino acid sequences are presented. The two .alpha.-chains differ in one residue at position 34 (Ala .fwdarw. Val) only. The primary structure of the chains was determined by sequencing the N-terminal regions (45 steps) and the tryptic peptides after their isolation from the digests by reversed-phase high-performance liquid chromatography. The alignment of these peptides was deduced from homology with other carnivora globins. The .alpha.-chain show 21 and the .beta.-chains 11 exchanges compared with human globin chains. In the .alpha.-chains, one heme- and two .alpha.1/.beta.1 contacts are exchanged. In the .beta.-chains there are three exchanges which involve one .alpha.1/.beta.1-, one .alpha.1/.beta.2- and one heme-contact. Between the ratel hemoglobin and those of carnivora a high degree of homology was found.

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