ABSTRACT: 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.

KEY WORDS: Cryptobia salmositica · Metallo-protease · Purification · Hydrolysis · Proteins

Published in DAO Vol. 30, No. 3 (1997) on September 30
ISSN: 0177-5103. Copyright © Inter-Research, Oldendorf/Luhe, 1997