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

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

Risultato della ricerca: Contributo in rivistaArticolo in rivista

10 Citazioni (Scopus)

Abstract

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.
Lingua originaleEnglish
pagine (da-a)261-268
Numero di pagine8
RivistaComparative Biochemistry and Physiology, Part B
Stato di pubblicazionePubblicato - 2004

Keywords

  • HEMOCYANIN

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