Eremin A N, Karaseva E I, Metelitsa D I
Prikl Biokhim Mikrobiol. 1989 Jul-Aug;25(4):524-31.
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.
在pH 7.4的缓冲生理溶液中，研究了抗孕酮抗体对葡萄糖-6-磷酸脱氢酶及其与孕酮结合物催化特性的影响。结合物中每个酶分子含有1 - 20个类固醇分子。在酶修饰程度较小时，若抗体过量，其活性会增加，而在相同条件下，含20个孕酮分子的结合物的催化活性降低了一半。在庚烷中的气溶胶OT和 Triton X - 45反胶束中，在存在抗孕酮抗体或非特异性抗血清（兔免疫球蛋白）的情况下，研究了含20个孕酮分子的葡萄糖-6-磷酸脱氢酶结合物催化活性的变化。在25℃、胶束极性相体积为6%且孵育时间较短时，两种抗血清均增加了结合物的活性，而在35℃、极性相体积为12%且孵育时间较长时，抗孕酮抗体显著降低了结合物的活性。
