Oberthür W, Braunitzer G, Baumann R, Wright P G
Hoppe Seylers Z Physiol Chem. 1983 Feb;364(2):119-34.
The primary structures of the alpha A- und beta-chains from the major hemoglobin component of the Ostrich (Struthio camelus) and American Rhea (Rhea americana) are given. The minor component with the alpha D-chains was detected in Ostrich in several concentrations, in American Rhea as in chicken and pheasant (about 40%). By homologous comparison, Greylag Goose (Anser anser) hemoglobin and Ostrich alpha A-chains differ by 15 amino acids or 16 nucleotide (1 two-point mutation) exchanges, beta-chains by 4 exchanges. Four substitutions modify alpha 1 beta 1-contacts and one phosphate contact. American Rhea and Greylag Goose hemoglobin alpha A-chains differ by 20 amino acids or 23 nucleotides (3 two-point mutations), beta-chains by 4 exchanges. Two substitutions modify alpha 1 beta 1-contacts, one phosphate contact and one heme contact. Oxygen affinity of three hemoglobin components of Ostrich are measured and the results are discussed. Systematic and evolution of Ostrich and American Rhea are discussed.
给出了鸵鸟（鸵鸟属骆驼鸵鸟）和美洲鸵鸟（美洲鸵鸟）主要血红蛋白成分的αA链和β链的一级结构。在鸵鸟中检测到几种浓度的含αD链的次要成分，在美洲鸵鸟中，其含量与鸡和雉鸡一样（约40%）。通过同源比较，灰雁（灰雁）血红蛋白与鸵鸟αA链有15个氨基酸或16个核苷酸（1个两点突变）的差异，β链有4个差异。四个替换改变了α1β1接触点和一个磷酸接触点。美洲鸵鸟和灰雁血红蛋白αA链有20个氨基酸或23个核苷酸（3个两点突变）的差异，β链有4个差异。两个替换改变了α1β1接触点、一个磷酸接触点和一个血红素接触点。测量了鸵鸟三种血红蛋白成分的氧亲和力并讨论了结果。讨论了鸵鸟和美洲鸵鸟的系统发育和进化。
