Isolation of acid protease from murine teratocarcinoma ascites fluid

An acid protease that appears responsible for causing cell-cell disaggregation in a mouse ascites teratocarcinoma was partially purified and characterized. The protease was purified from the mouse ascites fluid by affinity chromatography on Pepstatin A agarose beads. The purified material yielded one broad band on silver stained native polyacrylamide slab gels and two bands on silver stained SDS, 8-mercaptoethanol, slab gels, with approximate molecular weights of 66,000 and 20,000 Daltons. The affinity purification method yielded a 46 fold purification of the protease from the ascites fluid. These studies represent a first approach to purification and characterization of an enzyme that appears to be involved in altering the adhesiveness of a specific mouse ascites tumor.

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