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

Maria Teresa Sanna, Alessandra Olianas, Massimo Castagnola, Luigi Sollai, Barbara Manconi, Susanna Salvadori, Bruno Giardina, Magi Pellegrini

Research output: Contribution to journalArticle

10 Citations (Scopus)


The oxygen-binding properties of hexameric hemocyanin (He) 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 affinity constant of 1x10(4) M-1 were found and the exothermic contribution of their binding was found to be about 30 U mol(-1). Calcium ions largely influenced oxygen affinity: their effect, which has an opposite sign at low (0-1 mM) and high (0.1-1 M) concentration ranges, indicates the presence of two independent types of binding sites with high and low affinity, respectively; however, only the former ones seem to be operative in vivo because, at physiological calcium concentrations, they are already saturated and the oxygen affinity is reduced. (C) 2004 Elsevier Inc. All rights reserved.
Original languageEnglish
Pages (from-to)261-268
Number of pages8
JournalComparative Biochemistry and Physiology, Part B
Publication statusPublished - 2004




Dive into the research topics of 'Oxygen-binding modulation of hemocyanin from the slipper lobster Scyllarides latus'. Together they form a unique fingerprint.

Cite this