The primary structure of pale-throated three-toed sloth (Bradypus tridactylus, Xenarthra) hemoglobin.
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.
Max-Planck-Institut für Biochemie, Abteilung Proteinchemie, Martinsried bei München.
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T
Kleinschmidt
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März
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G
Braunitzer
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006454:Hemoglobins / Q000032:analysis*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012896:Sloths / Q000097:blood*; D004490:Xenarthra / Q000097:blood*
D000596:Amino Acids; D006454:Hemoglobins