[The primary structure of the hemoglobin gamma-chains of fetal sheep (Ovis ammon) and goat (Capra aegagrus), Artiodactyla].

The complete primary structures of the gamma-chains of fetal sheep (Ovis ammon) and goat (Capra aegagrus) hemoglobins are presented. The chains were isolated by chromatography on carboxymethyl cellulose CM-52. The primary structures of both chains were established by automatic Edman degradation, mainly on the tryptic peptides. The N-terminal regions were sequenced on the chains. Large C-terminal peptides were isolated and sequenced after acidic hydrolysis of the Asp-Pro bond (gamma 99/100). The peptides were aligned by their homology with the bovine gamma-chains. The gamma-chains of sheep and goat differ in 5 amino acid residues. Compared to bovine gamma-chains there are 12 and 10 exchanges, respectively. The influence of the primary structure on the intrinsic oxygen affinity of hemoglobins is discussed.