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Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen
Published on: March 4, 2017
Evaluation of the influence of temperature on the protein-tannic acid complex
Jéssica Miranda do Nascimento1, Talita Emanuely Henrique Leão1, Thiago Pajeú Nascimento2
1Laboratory of Research in Biotechnology and Hemoderivatives, Department of Pharmaceutical Sciences, Federal University of Pernambuco, 50670-420 Recife, Pernambuco, Brazil.
Abstract:
Precipitation of blood products from plasma fractionation has played a fundamental role in the industrial purification of important therapeutic products. Only a few studies have been reported by using tannins as proteins precipitant agent from whole plasma while, several conditions have been analyzed. Here, we decided to verify the effect of the temperature on the precipitation process of plasma proteins using tannic acid (TA). Plasma proteins were precipitated with tannic acid by using different temperature incubations. Subsequently, the protein-TA complex was analyzed by SDS-PAGE and quantified. In addition, the protein activity of the complex was measured after heating, as well as the structural changes of the complexes were accompanied by thermogravimetric analysis, differential scanning calorimetry and circular dichroism. In all conditions tested, tannic acid was able to precipitate without selectively separating the proteins in the mixture by using different temperatures during the precipitation process. Furthermore, the protein concentration from the plasma precipitate was not affected by different temperatures and the plasma precipitate was able to dissolve fibrin clots in vitro.
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