Caruso C, Rutigliano B, Romano M, di Prisco G
Institute of Protein Biochemistry and Enzymology, C.N.R., Naples, Italy.
Biochim Biophys Acta. 1991 Jun 24;1078(2):273-82. doi: 10.1016/0167-4838(91)90569-l.
The blood of the teleost Cygnodraco mawsoni, of the endemic Antarctic family Bathydraconidae, contains a major hemoglobin (Hb 1), accompanied by a minor component (Hb 2, about 5% of total). The two hemoglobins have identical alpha chains and differ by the beta chain. The complete amino acid sequence of the three chains has been elucidated, thus establishing the primary structure of both hemoglobins. The sequences show a 53-65% identity with non-Antarctic poikilotherm fish species; on the other hand, a very high degree of similarity (83-88%) has been found between Hb 1 and the major component of another Antarctic species of a different family. The hemoglobin functional properties relative to oxygen binding have been investigated in intact erythrocytes, 'stripped' hemolysate and purified components of C. mawsoni. The hemoglobins display the Bohr and Root effects, indicating fine regulation of oxygen binding by pH and by the physiological effectors organic phosphates.
南极特有的深龙科硬骨鱼马氏天鹅龙（Cygnodraco mawsoni）的血液中含有一种主要血红蛋白（Hb 1），还有一种次要成分（Hb 2，约占总量的5%）。这两种血红蛋白的α链相同，β链不同。已阐明了这三条链的完整氨基酸序列，从而确定了两种血红蛋白的一级结构。这些序列与非南极变温鱼类物种的序列有53 - 65%的同源性；另一方面，在Hb 1与另一个不同科的南极物种的主要成分之间发现了非常高的相似性（83 - 88%）。已对马氏天鹅龙完整红细胞、“脱辅基”溶血产物和纯化成分中与氧结合相关的血红蛋白功能特性进行了研究。这些血红蛋白表现出波尔效应和鲁特效应，表明pH值和生理效应物有机磷酸盐对氧结合有精细调节作用。
