High-altitude respiration of birds. The primary structures of the major and minor hemoglobin component of adult goshawk (Accipiter gentilis, Accipitrinae)

Biol Chem Hoppe Seyler. 1987 Apr;368(4):333-42. doi: 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.

MeSH terms

  • Altitude*
  • Amino Acid Sequence*
  • Animals
  • Birds / blood*
  • Chromatography, High Pressure Liquid
  • Electrophoresis, Polyacrylamide Gel
  • Hemoglobins / analysis*
  • Hemoglobins / isolation & purification
  • Phylogeny
  • Protein Conformation
  • Respiration*

Substances

  • Hemoglobins