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  • 1 University of Silesia A. Chełkowski’ Institute of Physics, Department of Medical Physics ul. Uniwersytecka 4 40-007 Katowice Poland
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Abstract  

A study of 2′,3′-dideoxyinosine (ddI) stability and its interaction with human serum albumin (HSA) was carried out by differential scanning microcalorimetry DSC. Scan rate dependent and irreversible endothermic thermal degradation of ddI was analyzed with use of kinetic approach. Observed process could be interpreted in terms of simple first-order one step kinetic model. Moreover it was shown that ddI bound weakly to the human serum albumin and stabilized this protein.

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