[Isolation and characterization of monoclonal antibodies to horseradish peroxidase].

Monoclonal antibodies to horseradish peroxidase were obtained. The interaction of two antibody clones with the enzyme was studied. Antibodies of one clone were found to inhibit the enzyme activity during the oxidation of 2.2'-azinobis-(3-ethylbenzothiazoline-6-sulfonate) diammonium salt and the cooxidation of luminol and luciferin. The latter was concomitant with a complete inhibition of the peroxidase activity. The values of binding constants as determined by the solid phase immunoenzymatic and homogeneous methods are equal to (1.2 +/- 0.5).10(8) M-1 and (1.8 +/- 0.2).10(11) M-1, respectively.