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The binding of concanavalin A in the dimer form to various saccharides has been studied by calorimetry, and estimates of the binding enthalpy and binding constants have been calculated. Methyl alpha-D-mannoside and methyl alpha-D-glucoside have a -- delta H0 of 21.5 and 11.5 kJ/mol, respectively, at both pH 4 and 4.5. The p-nitrophenyl derivatives react(More)
The thermal effects associated with the binding reaction of concanavalin A and immunoglobulins have been measured by calorimetry. IgG solutions do not generate heat on mixing with concanavalin A, confirming the low reactivity of IgG for the lectin molecule. IgM solutions, on the other hand, show a substantial enthalpic contribution of delta H = -24 +/-(More)
The reaction of concanavalin A with Mn2+ has been studied calorimetrically. The binding enthalpy was measured at two different temperatures, 25 and 30 degrees C, in 10(-3) M acetate buffer; it was found to be constant between pH 4.0 and 5.0, delta H250 = 95 kJ/mol and delta H300 = 65 kJ/mol, respectively. The two S1 binding sites are identical and(More)
A change in relaxation times has been determined in skin tissues after administration of hyaluramine, by means of nuclear magnetic resonance. Results are discussed in terms of water redistribution between the free and bound compartment.