[The sequence of the alpha- and beta-chains of the goldfish hemoglobin (Carassius auratus) (author's transl)].
The primary structures of the alpha- and beta-chains from goldfish hemoglobin are given. The globin chains were separated by gel filtration after oxidation of globin with air. The peptides for sequencing were obtained by chemical and enzymatical cleavage. The alpha-chain has 142 residues, the beta-chain 147. The alpha-chain is acetylated at the amino-terminal residue. Compared with the human chains, there are 66 amino acid differences in the alpha-chain, 72 residues are different in the beta-chain; the alpha-chain has no cysteine.
D000595:Amino Acid Sequence; D000818:Animals; D003530:Cyprinidae / Q000097:blood*; D006054:Goldfish / Q000097:blood*; D006454:Hemoglobins; D006801:Humans; D046911:Macromolecular Substances; D013045:Species Specificity
D006454:Hemoglobins; D046911:Macromolecular Substances
Die Sequenz der alpha- and beta-Ketten des Hämoglobins des Goldfisches (Carassius auratus).