Islam A, Beg O U, Persson B, Zaidi Z H, Jörnvall H
Department of Chemistry I, Karolinska Institutet, Stockholm, Sweden.
J Protein Chem. 1988 Oct;7(5):561-9. doi: 10.1007/BF01024874.
The structure of the hemoglobin alpha-chain of Rose-ringed Parakeet was determined by sequence degradations of the intact subunit, the CNBr fragments, and peptides obtained by digestion with staphylococcal Glu-specific protease and trypsin. Using this analysis, the complete alpha-chain structure of 21 avian species is known, permitting comparisons of the protein structure and of avian relationships. The structure exhibits differences from previously established avian alpha-chains at a total of 61 positions, five of which have residues unique to those of the parakeet (Ser-12, Gly-65, Ser-67, Ala-121, and Leu-134). The analysis defines hemoglobin variation within an additional avian order (Psittaciformes), demonstrates distant patterns for evaluation of relationships within other avian orders, and lends support to taxonomic conclusions from molecular data.
通过对完整亚基、溴化氰片段以及用葡萄球菌谷氨酸特异性蛋白酶和胰蛋白酶消化得到的肽段进行序列降解，确定了玫瑰环鹦鹉血红蛋白α链的结构。通过这种分析，已知21种鸟类的完整α链结构，从而可以比较蛋白质结构和鸟类之间的关系。该结构在总共61个位置上与先前确定的鸟类α链存在差异，其中5个位置具有鹦鹉特有的残基（Ser-12、Gly-65、Ser-67、Ala-121和Leu-134）。该分析确定了另外一个鸟类目（鹦形目）内的血红蛋白变异，展示了用于评估其他鸟类目内关系的远距离模式，并支持了来自分子数据的分类学结论。
