Oxygen binding characteristics of Oniscoidea hemocyanins (Crustacea; Terrestrial isopods)

Autor: Jean-G. Lagarrigue, Claude Sevilla
Rok vydání: 1979
Předmět:
Zdroj: Comparative Biochemistry and Physiology Part A: Physiology. 64:531-536
ISSN: 0300-9629
Popis: 1. 1. The pH of the Oniscoidea hemolymph is similar to those found in the Decapods. 2. 2. The oxygenation curves of the Oniscoidea hemocyanins are of sigmoidal shape under the experimental conditions used. 3. 3. The hemocyanins show a positive Bohr effect. The importance of this phenomenon varies according to the species. 4. 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 Oniscoidea hemocyanins. 5. 5. From an evolutionary viewpoint, there appears a general tendency towards a decrease of the affinities and oxygen binding capacities in the Oniscoidea hemocyanins with the various degrees of the species adaptation to the aerial respiration.
Databáze: OpenAIRE