Abstract
Actions of various chemical agents modeling immunoaffinity chromatography elution conditions caused structural changes of the components of human thyroid peroxidase (TPO) complexes with monoclonal antibodies (MABs) F8 and A1 whose antigenic determinants have a conformational nature and are located in the immunodominant region and a peripheral region of TPO, respectively. These changes became apparent in the circular dichroism and fluorescence spectra of TPO and both MABs as well as in the immunoassay. The effectiveness of the chemical reagents with respect to TPO desorption from an immobilized MAB decreased in the following order: 0.2 M ammonia (pH 11.5) > 0.1 M lithium 3,5-diiodosalycilate > 0.1 M glycine-HCl (pH 2.5) > 1 M NaI > 30% propylene glycol + 1 M NaCl > 30% propylene glycol > 1 M NaCl. At pH 11.5, the three-dimensional structure and immunoreactivity of TPO retained completely and only minor alterations of MAB analogical parameters took place, thus providing a high yield of the functional active human TPO and favoring repeated use of the immobilized MABs in immunoaffinity chromatography. The results may be used as a strategy for the optimization of various protein antigens immunoaffinity chromatography.
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Original Russian Text © E.P. Kiselyova, O.V. Tsyganova, I.I. Vashkevich, O.V. Sviridov, 2009, published in Prikladnaya Biokhimiya i Mikrobiologiya, 2009, Vol. 45, No. 3, pp. 369–377.
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Kiselyova, E.P., Tsyganova, O.V., Vashkevich, I.I. et al. Immunoaffinity chromatography of human thyroid peroxidase: The stability of the three-dimensional structure and immunoreactivity of antigen and antibodies under various elution conditions. Appl Biochem Microbiol 45, 334–342 (2009). https://doi.org/10.1134/S0003683809030168
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DOI: https://doi.org/10.1134/S0003683809030168