[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.
D000595:Amino Acid Sequence; D000818:Animals; D006041:Goats / Q000097:blood*; D006454:Hemoglobins; D046911:Macromolecular Substances; D010446:Peptide Fragments / Q000032:analysis; D012756:Sheep / Q000097:blood*; D013045:Species Specificity; D014357:Trypsin
D006454:Hemoglobins; D046911:Macromolecular Substances; D010446:Peptide Fragments; D014357:Trypsin
Die Primärstruktur der gamma-Ketten der fötalen Hämoglobine von Schaf (Ovis ammon) und Ziege (Capra aegagrus), Artiodactyla.