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The complete primary structures of two hemoglobin components of the European Souslik (Citellus citellus) are presented. The two hemoglobins have identical alpha-chains but differ in the amino-acid sequence of their beta-chains. The chain separation was achieved by chromatography on carboxymethyl-cellulose CM-52. Amino-acid sequences were established by automatic liquid-phase and gas-phase Edman degradation of the globin chains, of their tryptic peptides and of a peptide resulting from acidic hydrolysis of an Asp-Pro bond in the alpha-chain. The differences between the two beta-chains are manifested in three amino-acid exchanges. The sequences are compared with those of human and European Marmot hemoglobins. Only few differences were found among hemoglobins of C. citellus and other representatives of Sciuromorpha.

The Primary Structure of the Hemoglobin of the European Souslik (Citellus citellus, Rodentia)