Hiebl I, Kösters J, Braunitzer G
Biol Chem Hoppe Seyler. 1987 Apr;368(4):333-42. doi: 10.1515/bchm3.1987.368.1.333.
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.
本文展示了成年苍鹰（Accipiter gentilis）血红蛋白成分Hb A和Hb D的一级结构。球蛋白链在8M尿素缓冲液中于CM-纤维素上分离。通过在含NaCl线性梯度的磷酸盐缓冲液中，在TSK SP-5PW柱上进行快速蛋白质液相色谱（FPLC）分离成分。氨基酸序列通过在液相和气相测序仪中对球蛋白链及胰蛋白酶肽段进行自动埃德曼降解来确定。这些序列与欧洲黑兀鹫（Aegypius monachus）的序列比对。从序列数据推断苍鹰血红蛋白的系统发育方面及生理特性。在对隼形目应对极低氧分压的显著能力进行长期研究期间，已对氧结合特性进行了详细评估，这将是一篇即将发表论文的主题。
