Purification and characterization of particulate acid phosphatases from eggs of Mediterranean sea urchins

Abstract

1. 1. Particulate acid phosphatases were purified from unfertilized eggs of two Mediterranean sea urchins, Sphaerechinus granularis and Paracentrotus lividus. 2. 2. The apparent mol. wt of the enzyme was estimated to be approximately 700,000 and 600,000 for S. granularis and P. lividus, respectively, by gel filtration through Sepharose 4B and by polyacrylamide gel electrophoresis. 3. 3. The enzyme from both sources showed a glycoprotein nature with affinity chromatography on Concanavalin A-Sepharose 4B. 4. 4. Kinetic properties of the enzymes were similar to those from the eggs of Japanese and American sea urchins.