Ukr.Biochem.J. 2014; Volume 86, Issue 6, Nov-Dec, pp. 183-189
doi: https://doi.org/ 10.15407/ubj86.06.183
Avidity of polyreactive immunoglobulins
S. A. Bobrovnik
Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv;
e-mail: s-bobrov@bk.ru
An analysis of the mechanism of interaction between polyreactive immunoglobulins (PRIG) and antigen was conducted and it was shown that most of the traditional methods of antibody affinity evaluation are not applicable for PRIG affinity. The comparative assessment of the mouse and human PRIG avidity against ovalbumin and horse myoglobin and the avidity of specific monoclonal antibodies against ovalbumin have shown that the avidity of PRIG not only is much less than the avidity of monoclonal antibodies but even exceeds it.
Keywords: affinity, antibodies, antigen, avidity, polyreactive immunoglobulins
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