Tamburrini M, Brancaccio A, Ippoliti R, di Prisco G
Institute of Protein Biochemistry and Enzymology, C.N.R., Naples, Italy.
Arch Biochem Biophys. 1992 Jan;292(1):295-302. doi: 10.1016/0003-9861(92)90082-8.
The complete amino acid sequence of the single hemoglobin of the Antarctic teleost Gymnodraco acuticeps has been determined. The alpha chain contains 142 amino acid residues; an acetylated seryl residue is at the amino terminal. The beta chain contains 146 residues. A very high degree of sequence identity has been found with hemoglobins of other Antarctic fishes. Oxygen binding is not modulated by pH and allosteric effectors. The Bohr and Root effects are absent, although specific amino acid residues, considered responsible of most of these functions, are conserved in the sequence, thus posing new questions about the molecular basis of these mechanisms. The low heat of oxygenation may be interpreted as one of the mechanisms involved in the process of cold adaptation.
南极硬骨鱼裸头冰鱼单一血红蛋白的完整氨基酸序列已被确定。α链含有142个氨基酸残基；氨基末端为一个乙酰化的丝氨酸残基。β链含有146个残基。已发现其与其他南极鱼类的血红蛋白具有高度的序列同一性。氧结合不受pH值和别构效应剂的调节。不存在波尔效应和鲁特效应，尽管在序列中保留了被认为对这些功能中的大多数负责的特定氨基酸残基，因此这对这些机制的分子基础提出了新问题。低氧合热可被解释为参与冷适应过程的机制之一。
