Intrinsische Sauerstoffaffinität der Hämoglobine: Das Hämoglobin des Wisents(Bison bonasus,Bovidae)

Abstract
The hemoglobin from a European Bison (Bison bonasus) was analysed and the complete primary structures of the .alpha.1-, .alpha.II- and .beta.-chains have been determined. The .alpha.I- and .alpha.II-chains differ only at position .alpha.19 (Asp .fwdarw. Gly). The .beta.-chains are homogeneous. The sequences are compared with the globin chains of B. bison and bovine and the polymorphism of the .alpha.-chain is discussed. On the basis of the primary structure it may be concluded that the hemoglobin of .beta. sonasus belongs to the group of hemoglobins with intrinsically low oxygen affinity.