Oberthür W, Godovac-Zimmermann J, Braunitzer G, Wiesner H
Hoppe Seylers Z Physiol Chem. 1982 Aug;363(8):777-87. doi: 10.1515/bchm2.1982.363.2.777.
The amino acid sequences of the alpha- and beta-chains from the major hemoglobin component (HbA) of Canada goose (Branta canadensis) and mute swan (Cygnus olor) are given. The alpha-chains are of the alpha A-type, since alpha D-type was expressed but only found in low concentrations. By homologous comparison, greylag goose hemoglobin (Anser anser) and Canada goose hemoglobin alpha-chains differ by two exchanges, and beta-chains by three exchanges. A valine substitution for threonine was found at position alpha 34 (B15). This exchange is a result of a two point mutation. Thus, there are three nucleotide mutations in alpha-chains, as in beta-chains. Substitutions in positions alpha 34 (B15) and beta 125 (H3) have modified intersubunit contacts (alpha 1 beta 1-contacts). A comparison of mute swan hemoglobin with greylag goose hemoglobin shows four exchanges in alpha-chains and three in beta-chains. Canada goose and mute swan have identical beta-chains, while alpha-chains differ in two amino acids. One of these exchanges is implicated in one of the alpha 1 beta 1-contact points (alpha 34) where isoleucine substitution for valine was found. Comparison of hemoglobins from different species in the same tribe (Anserini) shows a high homology between Canada goose and mute swan hemoglobins.
给出了加拿大鹅（黑额黑雁）和疣鼻天鹅主要血红蛋白成分（HbA）的α链和β链的氨基酸序列。α链属于αA型，因为αD型虽有表达但仅在低浓度下被发现。通过同源比较，灰雁血红蛋白与加拿大鹅血红蛋白的α链有两处氨基酸交换差异，β链有三处氨基酸交换差异。在α34（B15）位置发现缬氨酸替代苏氨酸。这种交换是两点突变的结果。因此，α链和β链中都有三个核苷酸突变。α34（B15）和β125（H3）位置的替代改变了亚基间的接触（α1β1接触）。疣鼻天鹅血红蛋白与灰雁血红蛋白的比较显示，α链有四处氨基酸交换差异，β链有三处氨基酸交换差异。加拿大鹅和疣鼻天鹅的β链相同，而α链有两个氨基酸不同。其中一处交换涉及α1β1接触点之一（α34），在此处发现异亮氨酸替代缬氨酸。对同一族（雁族）不同物种的血红蛋白进行比较表明，加拿大鹅和疣鼻天鹅的血红蛋白具有高度同源性。
