A "living fossil" sequence: primary structure of the coelacanth (Latimeria chalumnae) hemoglobin--evolutionary and functional aspects.

@article{Gorr1991AF,
  title={A "living fossil" sequence: primary structure of the coelacanth (Latimeria chalumnae) hemoglobin--evolutionary and functional aspects.},
  author={Thomas Gorr and Traute Kleinschmidt and J G Sgouros and L Kasang},
  journal={Biological chemistry Hoppe-Seyler},
  year={1991},
  volume={372 8},
  pages={599-612}
}
The coelacanth (Latimeria chalumnae, Actinistia) has a single hemoglobin component. The primary structures of the alpha- and beta-chains are presented. They could be separated by reversed-phase HPLC. Peptides obtained by tryptic digestion of the native and oxidized chains were isolated by reversed-phase HPLC and sequenced in liquid and gas-phase sequenators. The alignment was achieved by employing the N-terminal sequences of the native chains and those of a beta-chain cyanogen bromide peptide… CONTINUE READING

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