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Binding Of Urate And Caffeine To Hemocyanin Analyzed By Isothermal Titration Calorimetry, Michael A. Menze, Nadja Hellmann, Heinz Decker, Manfred K. Grieshaber
Binding Of Urate And Caffeine To Hemocyanin Analyzed By Isothermal Titration Calorimetry, Michael A. Menze, Nadja Hellmann, Heinz Decker, Manfred K. Grieshaber
Michael Menze
Haemocyanin serves as an oxygen carrier in the haemolymph of decapod crustaceans. The oxygen-binding behaviour of the pigment is modulated by the two major anaerobic metabolites, L-lactate and urate. The binding of these two metabolites to haemocyanin has been investigated mainly indirectly by following the effectorinduced changes in the oxygen-binding properties of the respiratory pigment. Only a few direct investigations of effector binding, employing ultracentrifugation techniques and equilibrium dialysis, have been carried out. No evidence for cooperative binding for either effector was detected using these methods. However, isothermal titration calorimetry (ITC) offers a useful tool to gain additional insight into …
Binding Of Urate And Caffeine To Hemocyanin Of The Lobster Homarus Vulgaris (E.) As Studied By Isothermal Titration Calorimetry †, Michael A. Menze, Nadja Hellmann, Heinz Decker, Manfred K. Grieshaber
Binding Of Urate And Caffeine To Hemocyanin Of The Lobster Homarus Vulgaris (E.) As Studied By Isothermal Titration Calorimetry †, Michael A. Menze, Nadja Hellmann, Heinz Decker, Manfred K. Grieshaber
Michael Menze
Hemocyanin serves as an oxygen carrier in the hemolymph of the European lobster Homarus Vulgaris. The oxygen binding behavior of the pigment is modulated by metabolic effectors such as lactate and urate. Urate and caffeine binding to 12-meric hemocyanin (H. Vulgaris) was studied using isothermal titration calorimetry (ITC). Binding isotherms were determined for fully oxygenated hemocyanin between pH 7.55 and 8.15. No pH dependence of the binding parameters could be found for either effector. Since the magnitude of the Bohr effect depends on the urate concentration, the absence of any pH dependence of urate and caffeine binding to oxygenated hemocyanin …