title: The primary structure of the hemoglobin of the European Souslik (Citellus citellus, Rodentia).
abstract: 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.
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D005916:Globulins / Q000032:analysis; D006454:Hemoglobins / Q000032:analysis*; D006868:Hydrolysis; D012589:Sciuridae / Q000097:blood*; D014357:Trypsin
chemical_list: D000596:Amino Acids; D005916:Globulins; D006454:Hemoglobins; D014357:Trypsin