OBTAINING OF MONOCLONAL ANTIBODY FOR IMMUNOAFFINITY PURIFICATION OF MYELOPEROXIDASE AND PROTOTYPE OF HEMOSORBENT
Myeloperoxidase (MPO) is a promising target for anti-inflammatory therapy and prevention of atherosclerosis. It is known that MPO is an independent predictor of complications of cardiovascular pathologies, including secondary myocardial infarction. For developing an enzyme-linked immunoassay, we obtained monoclonal antibodies against MPO (clone 2F7), which, interacted with MPO according to the electrostatic principle according to the results of surface plasmon resonance analysis. When antibodies were immobilized on cyanogen bromide-activated agarose, the resulting sorbent selectively bound MPO at 0.15 M NaCl. The elution of MPO was provided by 1 M NaCl (pH 7.4), which did not disrupt the properties of the prosthetic heme group. When analyzing the sorption of MPO from plasma samples, the dissociation constant about 0.07 nM was determined. Given that the pathological concentration of MPO exceeds 0.15 nM, the resulting sorbent can be a prototype of a hemosorbent for MPO.