The complete amino-acid sequence of the major hemoglobin component (HbA) of the adult Northern Mallard (Anas platyrhynchos platyrhynchos) is presented. A minor component HbD was also detected but in low concentrations. The sequences of alpha A- and beta-chains were established by automatic Edman degradation on tryptic peptides and peptides obtained by specific chemical cleavages. The alignment of the peptides was performed by comparison with the alpha A- and beta-chains of Greylag Goose hemoglobin (Anser anser). Thereby an exchange of five positions in the alpha A-chains and three in the beta-chains was observed. No exchanges were found in the surroundings of the heme, in alpha 1 beta 2-contact points, or allosteric regulatory sites. In the alpha 1 beta 1-subunit interface one amino-acid residue in alpha A-chains and one in beta-chains are exchanged. By comparison with the amino-acid sequence derived from globin genes of Domestic Duck (Anas platyrhynchos), the alpha A-chains differ by two exchanges in the N-terminal region and the beta-chains by five exchanges the in C-terminal region. The comparison of the amino-acid sequence derived from alpha A-globin gene of the Moscovy Duck (Cairina moschata) and alpha A-chains of the Northern Mallard, shows only one replacement.