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Biol Chem Hoppe Seyler. 1989 Apr;370(4):303-8.

The primary structure of pale-throated three-toed sloth (Bradypus tridactylus, Xenarthra) hemoglobin.

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


The hemoglobin of the Pale-Throated Three-Toed Sloth (Bradypus tridactylus, Xenarthra) was separated into two components (ratio 4:1) with identical amino-acid analyses for the alpha- and beta-chains. The primary structures of both chains from the major component are given. They could be isolated by chromatography on carboxymethyl cellulose CM-52. The sequences have been determined by automatic Edman degradation of the native chains and their tryptic peptides. The comparison with human hemoglobin showed 27 substitutions in the alpha-chains and 33 in the beta-chains. In the alpha-chains one amino-acid exchange involves an alpha 1/beta 1-contact. In the beta-chains two heme- and four alpha 1/beta 1-contacts are substituted. The hemoglobin of the Sloth is compared to that of the Nine-Banded Armadillo (Dasypus novemcinctus), another representative of the order Xenerthra.

[Indexed for MEDLINE]

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