Carnivora: The Primary Structure of the Pacific Walrus (Odobenus rosmarus divergens,Pinnipedia) Hemoglobin

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Abstract
The primary structure of the .alpha.- and .beta.-chains of the hemoglobin from the Pacific Walrus (Odobenus rosmarus divergens, Pinnipedia) is presented. Sequence analysis revealed only one hemoglobin component whereas two bands were found in polyacrylamide gel electrophoresis. The globin chains were separated by high-performance liquid chromatography and the sequences determined by automatic liquid- and gas-phase sequencing of the chains and their tryptic peptides. The .alpha.-chains show 20 and the .beta.-chains 12 exchanges compared to the corresponding human chains. In the .alpha.-chains one heme- and two .alpha.1/.beta.1-contacts were exchanged whereas in the .beta.-chains one .alpha.1/.beta.1-, one .alpha.1/.beta.2- and one heme-contact are substituted. Compared to Harbour Seal (Phoca vitulina) the Walrus hemoglobin shows 9 amino-acid replacements in the .alpha.-chains and 5 in the .beta.-chains. The relation between Pinnipedia and Arctoidea is discussed.