DAO 30:177-185 (1997)  -  doi:10.3354/dao030177

The metallo-protease (200 kDa) from Cryptobia salmositica was purified using ion-exchange chromatography and gelfiltration. The purity of the enzyme was confirmed as there was only one homogeneous band using SDS-PAGE. Under in vitro conditions the purified metallo-protease completely degraded the extracellular matrix proteins (collagen types I, IV, V and laminin) and the membrane proteins isolated from rainbow trout erythrocytes. The results confirm that the C. salmositica metallo-protease is a histolytic enzyme and it contributes to salmonid cryptobiosis and to the direct transmission of the parasite between fish.

Cryptobia salmositica · Metallo-protease · Purification · Hydrolysis · Proteins