[Primary structure of hemoglobins of the musk rat (Ondatra zibethica, Rodentia)].
The amino-acid sequence for the hemoglobin of the musk-rat (Ondatra zibethica) was determined. The sequence of both chains was established by automatic Edman-Begg degradation of the tryptic peptides and, in the case of the beta-chains additionally of the prolyl-peptide. The complete primary structure of the alpha-chains differs at 22, that of the beta-chains at 36 positions from the adult human hemoglobin. There are no changes in the heme-binding residues, the alpha 1--beta 2 contact positions and the allosteric regulator sites. In the heme-pocket we found beta 44 Ser leads to His and 8 positions changed within the alpha 1--beta 1 contact regions. These changes are discussed with respect to the function of the respective regions.
D000595:Amino Acid Sequence; D000818:Animals; D003411:Arvicolinae / Q000097:blood*; D006441:Hemoglobin A; D006454:Hemoglobins; D006801:Humans; D046911:Macromolecular Substances; D010446:Peptide Fragments / Q000032:analysis; D013045:Species Specificity
D006454:Hemoglobins; D046911:Macromolecular Substances; D010446:Peptide Fragments; D006441:Hemoglobin A
Die Primärstruktur des Hämoglobins vom Bisam (Ondatra zibethica, Rodentia).