Carnivora: the primary structure of hemoglobin from the Masked Palm Civet (Paguma larvata, Viverridae).
The primary structure of the alpha- and beta-chains of hemoglobin from the Masked Palm Civet (Paguma larvata, Viverridae) is described. The chains were separated directly from hemoglobin by RP-HPLC. After tryptic digestion of the chains, the peptides were separated by RP-HPLC. Amino acid sequences were determined by Edman degradation in liquid and gas-phase sequencers. The alignment of the tryptic peptides was made by homology with human and other Carnivora hemoglobins. Paguma and human hemoglobin differ with respect to 23 amino-acid residues. Some of these amino-acid substitutions, which occur in both the alpha- and beta-chains, occur at contact sites between the subunits, and at the binding sites of heme and of organic phosphate, as well as involving residues responsible for the alkaline Bohr effect.
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Max-Planck-Institut für Biochemie, Abteilung Proteinchemie, Martinsried bei München.
Braunitzer
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Göltenboth
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D000595:Amino Acid Sequence; D000818:Animals; D002335:Carnivora / Q000097:blood*; D004912:Erythrocytes / Q000737:chemistry; D006454:Hemoglobins / Q000032:analysis*; D006801:Humans; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid
D006454:Hemoglobins