Rapid partial purification of placental glucocerebroside beta-glucosidase and its entrapment in liposomes.

1. A glucocerebroside beta-glucosidase-rich detergent-free preparation was obtained from human placentas by a rapid method combining affinity chromatography on concanavalin A-Sepharose and organic-solvent precipitation. In a typical preparation about 11000 units of the enzyme purified 1500-fold were obtained from five placentas in 2 days. 2. The enzyme preparation also contained other hydrolases, but the extent of their purification was much smaller. 3. Studies on entrapment in liposomes showed that all glucocerebroside beta-glucosidase activity used could be incorporated in neutral egg phosphatidylcholine-cholesterol liposomes. Association with liposomes appeared to discriminate against other proteins, including some of the hydrolases, thus contributing to further purification of the enzyme. More than 95% of the liposome-associated enzyme activity was latent.