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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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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.[1]

References

  1. Carnivora: the primary structure of hemoglobin from the Masked Palm Civet (Paguma larvata, Viverridae). He, C., Braunitzer, G., Göltenboth, R. Biol. Chem. Hoppe-Seyler (1990) [Pubmed]
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