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Journal of Experimental Biology 149,417-424 (1990)
Published by Company of Biologists 1990

THE INFLUENCE OF SALINITY ACCLIMATION ON THE TEMPERATURE SENSITIVITY OF OXYGEN BINDING TO THE HAEMOCYANIN OF THE PROSOBRANCH NEPTUNEA ANTIQUA

OLE BRIX 1, SAVERIO G. CONDO 2, ALFREDO COLOSIMO 3, and BRUNO GIARDINA 2

1 The Department of Zoology, Zoophysiological Laboratory, University of Aarhus, Denmark; Present address: Zoological Laboratory, University of Bergen, Allegaten 41, N-5007Bergen, Norway
2 The Department of Zoology, Zoophysiological Laboratory, University of Aarhus, Denmark; Present address: Department of Experimental Medicine and Biochemical Sciences, II University of Rome, Tor Vergata, Via Orazio Raimondo, 00173 Roma, Italy
3 The Department of Zoology, Zoophysiological Laboratory, University of Aarhus, Denmark; Present address: Department of Biochemistry, University of Chieti, 31100 Chieti, Italy

The thermal sensitivity of oxygen binding has been studied at 10, 15, 20 and 25 °C in whole blood from specimens of Neptunea antiqua acclimated to ambient salinities of 24 and 35{per thousand}. The O2 affinity is strongly pH-dependent, demonstrating a large reversed Bohr shift below pH8.0. The magnitude of the Bohr shift is not significantly influenced by temperature or ionic concentration. At 35{per thousand}, the blood O2-affinity is strongly influenced by temperature ({delta}Happ-{approx}58.6kJmol-1), while at 24{per thousand} there is almost no temperature sensitivity ({delta}Happ<-18.8kJmol-1)

Key words: gastropods, haemocyanin, oxygen binding, temperature tolerance

Accepted on November 28, 1989




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