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Catalytic activity of various steroid-peroxidase conjugates in aqueous and micellar media
A. N. Eryomin, O. G. Petrusha, V. D. Matveentzev, D. I. Metelitza
Institute of Bioorganic Chemistry, Academy of Sciences of the Byelorussian SSR, Minsk
Abstract: The horseradish peroxidase (HRP) conjugates with the sheep antirabbit antibodies and cortisol (COR) or progesterone (PROG) containing 9 to 40 steroid molecules per HRP molecule were synthesized. In aqueous media all the conjugates have lower catalytic activity in the o-phenylenediamine oxidation than the native enzyme. In reversed Aerosol OT micelles in heptane the HRP–COR and HRP–PROG conjugates containing 12 and 9 steroid molecules, respectively, have catalytic constants 2.6 and 2.7 times higher than the unmodified enzyme. The influence of the HRP hydrophobisation and its inactivation on the course of modification on catalytic properties of the enzyme is discussed.
Russian Journal of Bioorganic Chemistry 1990, 16 (12):1629-1636