[Catalytic activity of conjugates of glucose-6-phosphate dehydrogenase with progesterone in aqueous and micellar media in the presence of specific and non-specific antibodies].

The effect of antibodies against progesterone on catalytic properties of glucose-6-phosphate dehydrogenase and its conjugates with progesterone was studied in the buffered physiological solution, pH 7.4. The conjugates contained 1-20 molecules of the steroid per enzyme molecule. At small degrees of the enzyme modification its activity increased in case of excess antibodies, while the catalytic activity of the conjugate with 20 progesterone molecules decreased twice under the same conditions. Change in the catalytic activity of glucose-6-phosphate dehydrogenase conjugates with 20 progesterone molecules was studied in Aerosol OT and Triton X-45 reversed micelles in heptane in the presence of antibodies against progesterone or a nonspecific antiserum (rabbit immunoglobulins). Both the antisera increased the conjugate activity at 25 degrees, 6% volume of the micelle polar phase, and short incubation, while at 35 degrees, 12% volume of the polar phase and long incubation the antibodies against progesterone significantly decreased the conjugate activity.