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- W2039179818 abstract "1. The pH of the Oniscoïdea hemolymph is similar to those found in the Decapods. 2. The oxygenation curves of the Oniscoïdea hemocyanins are of sigmoïdal shape under the experimental conditions used. 3. The hemocyanins show a positive Böhr effect. The importance of this phenomenon varies according to the species. 4. The hemocyanins present (concerning their affinity and oxygen binding capacity) a different sensibility to the presence of Ca2+ and Mg2+ in the medium. The divalent cations intensify the interaction degree between the oxygen binding sites in all the Oniscoïdea hemocyanins. 5. From an evolutionary viewpoint, there appears a general tendency towards a decrease of the affinities and oxygen binding capacities in the Oniscoïdea hemocyanins with the various degrees of the species adaptation to the aerial respiration." @default.
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- W2039179818 date "1979-01-01" @default.
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- W2039179818 title "Oxygen binding characteristics of Oniscoidea hemocyanins (Crustacea; Terrestrial isopods)" @default.
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- W2039179818 doi "https://doi.org/10.1016/0300-9629(79)90579-6" @default.
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