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

The thermal denaturation process of bovine and human both fatty acid containing and fatty acid free albumins in aqueous solution was studied by use of differential scanning calorimetry. Human serum albumins were found to be more stable than their bovine counterparts. Fatty acid free albumins were characterized as generally less stable, more susceptible to aggregation, their unfolding endothermic transition was less cooperative and with the smaller degree of reversibility. Deconvolution analysis with using a non-two-state model with two component transitions showed essential differences in the thermodynamic parameters between all studied albumins, particularly regarding the high-temperature component transition.

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