Dettaï Agnes, di Prisco Guido, Lecointre Guillaume, Parisi Elio, Verde Cinzia
UMR, Département Systématique et Evolution, Muséum National d'Histoire Naturelle, Paris, France.
Methods Enzymol. 2008;436:539-70. doi: 10.1016/S0076-6879(08)36030-3.
Because hemoglobins (Hbs) of all animal species have the same heme group, differences in their properties, including oxygen affinity, electrophoretic mobility, and pH sensitivity, must result from the interaction of the prosthetic group with specific amino acid residues in the primary structure. For this reason, fish globins have been the object of extensive studies in the past few years, not only for their structural characteristics but also because they offer the possibility to investigate the evolutionary history of Hbs in marine and freshwater species living in a large variety of environmental conditions. For such a purpose, phylogenetic analysis of globin sequences can be combined with knowledge of the phylogenetic relationships between species. In addition, Type I functional-divergence analysis is aimed toward predicting the amino acid residues that are more likely responsible for biochemical diversification of different Hb families. These residues, mapped on the three-dimensional Hb structure, can provide insights into functional and structural divergence.
由于所有动物物种的血红蛋白（Hb）都具有相同的血红素基团，其特性（包括氧亲和力、电泳迁移率和pH敏感性）的差异必定源于辅基与一级结构中特定氨基酸残基的相互作用。因此，鱼类球蛋白在过去几年一直是广泛研究的对象，这不仅是因为它们的结构特征，还因为它们提供了研究生活在各种环境条件下的海洋和淡水物种中血红蛋白进化历史的可能性。出于这一目的，球蛋白序列的系统发育分析可以与物种间系统发育关系的知识相结合。此外，I型功能差异分析旨在预测更可能导致不同血红蛋白家族生化多样化的氨基酸残基。这些残基映射在血红蛋白的三维结构上，可以为功能和结构差异提供见解。
