Oxygen-binding modulation of hemocyanin from the slipper lobster Scyllarides latus.

@article{Sanna2004OxygenbindingMO,
  title={Oxygen-binding modulation of hemocyanin from the slipper lobster Scyllarides latus.},
  author={Maria Teresa Sanna and Alessandra Olianas and Massimo Castagnola and Luigi Sollai and Barbara Manconi and Susanna Salvadori and Bruno Giardina and Mariagiuseppina Pellegrini},
  journal={Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology},
  year={2004},
  volume={139 2},
  pages={261-8}
}
The oxygen-binding properties of hexameric hemocyanin (Hc) from Scyllarides latus were investigated with respect to pH, temperature, and modulating effect exerted by calcium, lactate, and urate. The oxygen affinity decreased at higher temperature, was slightly affected by pH, and was insensitive to lactate. Nevertheless, urate markedly increased Hc-oxygen affinity and its temperature sensitivity, acting as the physiological major positive effector: four urate sites per hexamer with an overall… CONTINUE READING