[Intrinsic oxygen affinity of hemoglobins: the hemoglobin of bisons (Bison bonasus,Bovidae)].
The hemoglobin from a European Bison (Bison bonasus) was analysed and the complete primary structures of the alpha I-, alpha II-and beta-chains have been determined. The alpha I- and alpha II-chains differ only at position alpha 19 (Asp----Gly). The beta-chains are homogeneous. The sequences are compared with the globin chains of Bison bison and bovine and the polymorphism of the alpha-chains is discussed. On the basis of the primary structure it may be concluded that the hemoglobin of Bison bonasus belongs to the group of hemoglobins with intrinsically low oxygen affinity.
D000595:Amino Acid Sequence; D000818:Animals; D001188:Artiodactyla / Q000097:blood*; D004591:Electrophoresis, Polyacrylamide Gel; D005914:Globins / Q000032:analysis*; D010100:Oxygen / Q000097:blood; D010108:Oxyhemoglobins / Q000378:metabolism*; D011110:Polymorphism, Genetic
D010108:Oxyhemoglobins; D005914:Globins; D010100:Oxygen
Intrinsische Sauerstoffaffinität der Hämoglobine: Das Hämoglobin des Wisents (Bison bonasus, Bovidae).