6533b857fe1ef96bd12b4601
RESEARCH PRODUCT
Temperature adaptation influences the aggregation state of hemocyanin from Astacus leptodactylus.
Roman FöllHeinz Deckersubject
PhysiologyEcologymedicine.medical_treatmentProtein subunitTemperatureCooperativityHemocyaninBohr effectmacromolecular substancesBiologyHydrogen-Ion ConcentrationAstacus leptodactylusbiology.organism_classificationBiochemistryAdaptation PhysiologicalCrustaceaHemolymphHemocyaninsmedicineBiophysicsAnimalsElectrophoresis Polyacrylamide GelAdaptationMolecular BiologyOxygen bindingdescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2000-10-01 | Comparative biochemistry and physiology. Part A, Molecularintegrative physiology |