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Abstract  

Human serum albumin unfolding in ethanol/water mixtures was studied by use of differential scanning calorimetry. Ethanol-induced changes in DSC curves of defatted and non-defatted albumin were markedly different. In the presence of ethanol, bimodal denaturation transition for fatty acid free albumin was observed while that for albumin containing endogenous fatty acids was single and more sharpen than in aqueous solution. Ethanol was found to decrease the thermal stability of albumin due to the binding to the unfolded state to a higher degree than to the native state, thus favouring unfolding. The binding with different affinities has been suggested depending on ethanol concentration range.

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Abstract  

The effect of ethanol on human serum albumin stability in aqueous solution was studied by use of differential scanning calorimetry. A deconvolution of DSC traces in 2-state model with ΔC p=0 and ΔC p≠0 was performed and analysed to obtain information on the interaction of ethanol with different parts of albumin molecule both fatty acid containing and fatty acid free. The differences in ethanol binding affinity for both kinds of albumin were found. At very low concentrations ethanol was observed to be a stabilizer of the folded state of albumin contrary to the higher concentration where its binding to the unfolded protein predominates.

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