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Stability of bovine serum albumin at different pH |
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| Authors: | Anna Michnik Katarzyna Michalik Zofia Drzazga |
| Affiliation: | (1) University of Silesia, A. Chełkowski' Institute of Physics, Dpt. of Medical Physics, ul. Universytecka 4, Katowice, 40-007 Poland;(2) University of Silesia, A. Chełkowski' Institute of Physics, Dpt. of Medical Physics, ul. Universytecka 4, Katowice, 40-007 Poland;(3) University of Silesia, A. Chełkowski' Institute of Physics, Dpt. of Medical Physics, ul. Universytecka 4, Katowice, 40-007 Poland |
| Abstract: | Summary The effect of pH on the thermal denaturation of BSA containing fatty acids was studied by use of differential scanning calorimetry (DSC). Thermal scanning of BSA aqueous solutions gave various types of DSC curves depending on the protein concentration and on the pH. The broad bimodal endothermic transition was suggested to be connected with loose protein structure in contradistinction to single peak for compact molecule structure. The propensity toward precipitation at pH conditions ranging from 3.8 to 5 was observed. A scan-rate independent and partly reversible behavior of the thermal heating of BSA was found. Deconvolution of DSC traces in non-two-state model with assumption of two- or three-component transition allowed to study the effect of pH on different parts of BSA molecule. |
| Keywords: | DSC thermal stability bovine serum albumin protein denaturation |
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