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Biol Chem Hoppe Seyler. 1990 Oct;371(10):1015-20.

Carnivora: the primary structure of hemoglobin from the Masked Palm Civet (Paguma larvata, Viverridae).

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Max-Planck-Institut für Biochemie, Abteilung Proteinchemie, Martinsried bei München.


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.

[Indexed for MEDLINE]

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