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‰. 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‰, the blood O2-affinity is strongly influenced by temperature (δHapp-≈58.6kJmol−1), while at 24‰ there is almost no temperature sensitivity.
Oxygen-binding properties of Cephalopod blood with special reference to environmental temperatures and ecological destribution / Brix, O.; Condo, S. G.; Colosimo, Alfredo; Giardina, B.. - In: JOURNAL OF EXPERIMENTAL BIOLOGY. - ISSN 0022-0949. - STAMPA. - 205:(1990), pp. 253-263.
Oxygen-binding properties of Cephalopod blood with special reference to environmental temperatures and ecological destribution.
COLOSIMO, Alfredo;
1990
Abstract
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‰. 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‰, the blood O2-affinity is strongly influenced by temperature (δHapp-≈58.6kJmol−1), while at 24‰ there is almost no temperature sensitivity.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
