Haemoglobin of the antarctic fish Pagothenia bernacchii. Amino acid sequence, oxygen equilibria and crystal structure of its carbonmonoxy derivative.

@article{Camardella1992HaemoglobinOT,
  title={Haemoglobin of the antarctic fish Pagothenia bernacchii. Amino acid sequence, oxygen equilibria and crystal structure of its carbonmonoxy derivative.},
  author={Laura Camardella and Carla Caruso and Rossana D'Avino and Guido di Prisco and B Rutigliano and Maurizio Tamburrini and Giuilio Fermi and Max F. Perutz},
  journal={Journal of molecular biology},
  year={1992},
  volume={224 2},
  pages={449-60}
}
The Antarctic fish Pagothenia bernacchii has one major haemoglobin, Hb1 (over 95% of the total blood content). Hb1 has a strong alkaline Bohr effect and at low pH exhibits the reduced ligand affinity and co-operativity that comprise the Root effect. We have determined the complete amino acid sequence of P. bernacchii Hb1 and also the structure of its carbonmonoxy derivative by X-ray crystallography, to a resolution of 2.5 A. The crystallographic R-factor of the refined structure is 18%. The… CONTINUE READING

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