Oberthür W, Braunitzer G, Würdinger I
Hoppe Seylers Z Physiol Chem. 1982 Jun;363(6):581-90.
The primary structures of the alpha- and beta-chains of the main component of Bar-headed Goose (Anser indicus) are given. By homologous comparison with the hemoglobin of the Grey-Lag Goose (Anser anser) 3 differences were found in the alpha-chains, 1 difference in the beta-chains. In position alpha 119 H2Ala and beta 125 H3Asp alpha 1 beta 2-contact points are changed. The mutation alpha 63 E12Val brings a drastic change in tertiary structure of the alpha-chains of Bar-headed Goose: the helices E and B are moved apart by 1.5 A as there is no room for the larger side chain. This is probably the reason for a slightly higher intrinsic oxygen affinity of Bar-headed Goose hemoglobin. The bindings of inositol pentaphosphate on hemoglobin are identical in Grey-Lag Goose and Bar-headed Goose (contact points are not mutated). The reason for the increased difference in oxygen affinity by binding of inositol pentaphosphate is probably caused by two mutations in alpha 1 beta 2-contact points. It suggests that these two mutations are the reason for a different interaction between alpha- and beta-chains under the influence of inositol pentaphosphate by Grey-Lag and Bar-headed Goose hemoglobins. The difference in the primary structure of the Grey-Lag and Bar-headed Goose hemoglobins suggests that the Bar-headed Goose is not the genus of anser. Unfinished experiments (about 80% of the sequences) of White-fronted Goose (Anser albifrons a.) and Snow Goose (Anser caerulescens c.) show no exchanges with Grey-Lag Goose hemoglobin. The Canada Goose (Branta canadensis), however, which belongs to the genus Branta, has a number of substitutions similar to the Bar-headed Goose hemoglobin. These changes in primary structure suggest that Grey-Lag Goose and Bar-headed Goose are separated by a period of 9-15 Million years. This would support the hypothesis that the two species of goose became geographically separated by the elevation of the Himalayas.
给出了斑头雁（Anser indicus）主要成分的α链和β链的一级结构。通过与灰雁（Anser anser）的血红蛋白进行同源比较，发现α链中有3个差异，β链中有1个差异。在α119 H2Ala和β125 H3Asp位置，α1β2接触点发生了变化。α63 E12Val突变使斑头雁α链的三级结构发生了剧烈变化：由于没有空间容纳较大的侧链，E螺旋和B螺旋分开了1.5埃。这可能是斑头雁血红蛋白内在氧亲和力略高的原因。灰雁和斑头雁血红蛋白上肌醇五磷酸的结合是相同的（接触点未发生突变）。肌醇五磷酸结合导致氧亲和力差异增加的原因可能是α1β2接触点的两个突变。这表明这两个突变是灰雁和斑头雁血红蛋白在肌醇五磷酸影响下α链和β链之间不同相互作用的原因。灰雁和斑头雁血红蛋白一级结构的差异表明斑头雁不属于雁属。对白额雁（Anser albifrons a.）和雪雁（Anser caerulescens c.）未完成的实验（约80%的序列）表明，它们与灰雁血红蛋白没有交换。然而，属于黑雁属的加拿大雁（Branta canadensis）有一些与斑头雁血红蛋白相似的替代。一级结构的这些变化表明，灰雁和斑头雁在900万至1500万年前就已分离。这将支持这样一种假设，即这两种鹅由于喜马拉雅山脉的隆起而在地理上分离。
