Abstract
α-Mannosidase [EG 3.2.1.24] was purified 90-fold from the liver of Charonia lampas, using p-nitrophenyl α-D-mannoside as substrate. The enzymological properties of the purified enzyme are described. The purified a-mannosidase was practically free from other various glycosidases tested and it produced mannose from ovalbumin glycopeptide. A mixture of partially purified glycosidases was obtained from the liver of the gastropod, using Sephadex G-200 column chromatography.