Differential Scanning Calorimetric Study of Bovine Insulin.
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概要
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The thermal unfolding of insulin was studied at various pHs by an adiabatic DSC. The involvement of self-association of insulin in both folded and unfolded sates caused complex profiles in DSC curves. The exothermic heat effect due to the aggregation of the unfolded molecule was found to be associated with the endothermic heat effect due to the unfolding of native insulin at neutral pH and at pHs below 2. At a pH range from 2 to 4.5, the unfolding was quantitatively reversible. DSC curves observed in acetic acid solution where the molecular association is negligible showed a broad peak indicating that the monomeric insulin has a relatively loose structure in the aspect of thermodynamic cooperativity.
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