[The primary structure of hemoglobins from the bottlenosed dolphin (Tursiops truncatus, Cetacea)].

@article{Kleinschmidt1983ThePS,
  title={[The primary structure of hemoglobins from the bottlenosed dolphin (Tursiops truncatus, Cetacea)].},
  author={Traute Kleinschmidt and Gerhard Braunitzer},
  journal={Biomedica biochimica acta},
  year={1983},
  volume={42 6},
  pages={685-95}
}
Only one hemoglobin component was found in the bottlenosed dolphin (Tursiops truncatus, Cetacea). The alpha and beta chains were separated by chromatography on CM-52 cellulose. The complete primary structures of both chains were established by automatic Edman degradation of the chains and the tryptic peptides. The alignment was done by homology with alpha und beta chains of adult human hemoglobin. A comparison of these two hemoglobins shows an exchange of 22 amino acid residues in the alpha… CONTINUE READING