Braunitzer G, Oberthür W
Hoppe Seylers Z Physiol Chem. 1979 May;360(5):679-83.
The primary structures of the alpha- and beta-chains from greylag goose (Anser anser) hemoglobin are given. The sequence was deduced automatically in the sequenator. They differ from chicken alpha-chains in the exchange of 30, from beta-chains in the exchange of only 8 amino acid residues, respectively. The contact points of inositol pentaphosphate with the beta-chains are identical in chicken and greylag goose. Unequal evolution of the beta-chains was found, which is published here for the first time. By comparing the sequences of chicken and greylag goose and considering paleontological data, we found the mutation rate of the alpha-chains to be normal, i.e. 6 million years/mutation. This corresponds to the values for other species. The mutation rate of beta-chains is reduced and was calculated at 25 million years/mutation. This is possibly due to a specific function of beta-chains. This paper is the basis of our attempt to explain on a molecular basis the ability of bar-headed goose (Anser indicus) to fly and breathe at high altitudes.
给出了灰雁(Anser anser)血红蛋白α链和β链的一级结构。序列是在测序仪中自动推导出来的。它们与鸡的α链分别在30个氨基酸残基的替换上存在差异,与β链仅在8个氨基酸残基的替换上存在差异。肌醇五磷酸与β链的接触点在鸡和灰雁中是相同的。发现了β链的不均衡进化,这在此处首次发表。通过比较鸡和灰雁的序列并考虑古生物学数据,我们发现α链的突变率是正常的,即每600万年发生一次突变。这与其他物种的值相对应。β链的突变率降低,经计算为每2500万年发生一次突变。这可能是由于β链的特定功能所致。本文是我们试图从分子层面解释斑头雁(Anser indicus)在高海拔地区飞行和呼吸能力的基础。