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

1 January 1987

journal article
research article
Published by Walter de Gruyter GmbH in Biological Chemistry Hoppe-Seyler

Vol. 368 (1) , 333-342
https://doi.org/10.1515/bchm3.1987.368.1.333

Abstract

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.

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