Temperature adaptation influences the aggregation state of hemocyanin from Astacus leptodactylus.
When Astacus leptodactylus were kept at various temperatures for several weeks, different ratios between di-hexameric and hexameric hemocyanins were observed in their hemolymph. The higher the temperature the more hexamers were present. This long-term adaptation to different temperatures or/and to temperature-induced pH-shifts as observed in the hemolymph has different effects on the expression of subunit types building up hexamers and those which covalently link two hexamers within the di-hexamers. The oxygen binding behaviour of di-hexameric hemocyanins from cold and warm adapted animals do not show differences with respect to affinity, Bohr effect and cooperativity.
Decker
H
H
Institute for Molecular Biophysics, University of MainzJacob Welder Weg 26, D-55099, Mainz, Germany. decker@biophysik.biologie.uni-mainz.de
Föll
R
R
D000222:Adaptation, Physiological; D000818:Animals; D003445:Crustacea / Q000378:metabolism / Q000502:physiology*; D004591:Electrophoresis, Polyacrylamide Gel; D006433:Hemocyanins / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D013696:Temperature
D006433:Hemocyanins