Enhanced solubilization of polygalacturonic acid synthase by ribonuclease treatment of cell homogenates

The glycosyltransferases involved in plant cell wall biosynthesis are generally too low in concentration to allow for their purification. Therefore, the development of a method for enhanced solubilization of membrane proteins is necessary. Here, we report ribonuclease treatment of cell homogenates of azuki bean epicotyls. Polygalacturonic acid synthase, localized at the plant Golgi membrane, was enriched 2.0-fold in specific activity after ribonuclease treatment. Total enzyme activity per unit weight was also improved 2.1-fold. These data indicate that ribonuclease works to remove ribosomes from the microsomal fraction and enhances the solubilization of polygalacturonic acid synthase.