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  • Title: [Primary structure of hemoglobins of the musk rat (Ondatra zibethica, Rodentia)].
    Author: Bieber FA, Braunitzer G.
    Journal: Hoppe Seylers Z Physiol Chem; 1983 Nov; 364(11):1527-36. PubMed ID: 6363267.
    Abstract:
    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.
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