| Abstract: | Conditions for copolymerization of native and sodium periodate-oxidized horseradish peroxidase (HTP; EC 1.11.1.7) have been optimized. Copolymerization products have been characterized electrophoretically, spectrally, and kinetically. Copolymers containing 2-3, 4, 5-7, and 9-10 molecules of the enzyme were found among the products of polymerization. The copolymers had lower values of D403/D280 than HRP. The copolymers had more ordered structures than the original HRP. Comparison of the thermal stability and kinetic characteristics of the fractions differing in the ratio of copolymers to the monomeric enzyme demonstrated that the polymeric products were more stable than HRP (in terms of resistance to high temperature or inhibitory effects of H202), but their kinetic activity was, on the whole, lower than that of the original enzyme. |
