The primary structures of the hemoglobin components Hb A and Hb D of the European Black Vulture (Aegypius monachus) are presented. The globin chains were separated on CM-Cellulose in 8M urea buffer. The amino-acid sequences were established by automatic Edman degradation of the globin chains and the tryptic peptides in liquid phase and gas-phase sequenators. The sequences are compared with those of the Golden Eagle, and with those of the Andean Condor, a New World vulture. The possible evolutionary significance of the alpha D-chains is considered. This paper serves as a reference study for high-altitude respiration of Falconiformes.