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The primary structures of the hemoglobin components Hb A and Hb D of the adult Goshawk (Accipiter gentilis) are presented. The globin chains were separated on CM-Cellulose in 8M urea buffer. Component separation was achieved by FPLC-chromatography on a TSK SP-5PW column in phosphate-buffers with a linear gradient of NaCl. The amino-acid sequences were established by automated Edman degradation of the globin chains and of the tryptic peptides in liquid-phase and gas-phase sequenators. The sequences are aligned with those of European Black Vulture (Aegypius monachus). Phylogenetic aspects and physiological properties for Goshawk hemoglobin are inferred from sequence data. A detailed evaluation of the oxygen-binding properties has been carried out during a prolonged study of the noteworthy ability of Falconiformes to cope with extremely low oxygen partial pressures, and will be the subject of a forthcoming paper.

biological chemistry hoppe-seyler

High-Altitude Respiration of Birds. The Primary Structures of the Major and Minor Hemoglobin Component of Adult Goshawk ( Accipiter gentilis,  Accipitrinae)