D'Avino R, Di Prisco G
Institute of Protein Biochemistry and Enzymology, Consiglio Nazionale delle Ricerche, Naples, Italy.
Eur J Biochem. 1989 Feb 15;179(3):699-705. doi: 10.1111/j.1432-1033.1989.tb14603.x.
Antarctic fishes live at a constant temperature of -1.8 degrees C, in an oxygen-rich environment. In comparison with fishes that live in temperate or tropical waters, their blood contains less erythrocytes and hemoglobin. A study was initiated on the structure and function of Antarctic fish hemoglobin. The erythrocytes of the Antarctic benthic teleost Notothenia coriiceps neglecta, of the family Nototheniidae, have been shown to contain two hemoglobins, accounting for about 90% and 5% of the total content. These hemoglobins have been isolated, and obtained in crystalline form. They are tetramers and contain two pairs of globin chains. The globin chains of each hemoglobin have been purified and characterised. The two hemoglobins appear to have one of the two globin chains in common. The Root and Bohr effects have been investigated in erythrocytes, 'stripped' hemolysates and pure hemoglobins, indicating that the functional properties are finely regulated by pH and allosteric effectors.
南极鱼类生活在恒定温度为零下1.8摄氏度且氧气丰富的环境中。与生活在温带或热带水域的鱼类相比，它们的血液中红细胞和血红蛋白含量较少。一项关于南极鱼类血红蛋白结构和功能的研究启动了。南极底栖硬骨鱼科的小头南极鱼的红细胞已被证明含有两种血红蛋白，分别约占总含量的90%和5%。这些血红蛋白已被分离出来，并获得了晶体形式。它们是四聚体，包含两对球蛋白链。每种血红蛋白的球蛋白链已被纯化并表征。这两种血红蛋白似乎有一条球蛋白链是相同的。已经在红细胞、“去除其他物质的”溶血产物和纯血红蛋白中研究了鲁特效应和波尔效应，表明其功能特性受到pH值和变构效应剂的精细调节。
