Oberthür W, Braunitzer G, Kalas S
Hoppe Seylers Z Physiol Chem. 1981 Aug;362(8):1101-12.
The alpha- and beta-chains of the main component of hemoglobin of the greylag goose (Anser anser) were isolated. For determination of the primary structure of hemoglobin, the chains were cleaved and the cleavage products isolated. The chains and peptides were degraded automatically in the sequenator: the complete primary structure of the alpha-and beta-chains was obtained and compared with the human adult hemoglobin. Comparison with human sequences show 1 substitutions in the alpha-chain and 44 in beta-chain. The mutations are discussed. The alpha-chains contain no tryptophan, only one methionine and two cysteines. Seven alpha 1 beta 1-contacts and one alpha 1 beta 2-oxy- and deoxy-contact are altered. In the beta-chains two acidic amino acids are eliminated. This is probably the reason for the more basic character of the greylag goose hemoglobin. The contact points of the allosteric effector (inositol pentaphosphate in case of birds, 2,3-diphosphoglycerate in case of mamals) with the beta-chains are identical in chicken and greylag goose, two more than in the human beta-chains. Six alpha 1 beta 1-contacts and one hem-contact are changed. This work forms a basis to allow comparison of the functions of several bird hemoglobins and for further studies of bird hemoglobins and for further studies of evolution and systematics of birds.
灰雁（Anser anser）血红蛋白主要成分的α链和β链被分离出来。为了确定血红蛋白的一级结构，将这些链进行切割并分离出切割产物。这些链和肽在测序仪中自动降解：获得了α链和β链的完整一级结构，并与成人血红蛋白进行了比较。与人类序列的比较显示，α链中有1个取代，β链中有44个取代。对这些突变进行了讨论。α链不含色氨酸，只有一个甲硫氨酸和两个半胱氨酸。七个α1β1接触点以及一个α1β2氧合和脱氧接触点发生了改变。在β链中，两个酸性氨基酸被去除。这可能是灰雁血红蛋白碱性更强的原因。变构效应物（鸟类为肌醇五磷酸，哺乳动物为2,3-二磷酸甘油酸）与β链的接触点在鸡和灰雁中是相同的，比人类β链多两个。六个α1β1接触点和一个血红素接触点发生了变化。这项工作为比较几种鸟类血红蛋白的功能以及进一步研究鸟类血红蛋白、鸟类的进化和系统发育奠定了基础。
