The complete primary structure of the hemoglobin from the adult coati (Nasua nasua rufa) is presented. The erythrocytes contain one hemoglobin component and two globin chains. The isolation of globin chains was achieved by reversed-phase HPLC on a column of Nucleosil-C4. The primary structures of globin chains and tryptic peptides was determined in liquid- and gas-phase sequenators. The sequence of the alpha and beta-chains of coati compared with those of other Carnivora species. Results are discussed with respect to structural variations and the phylogenetic relationship.