Abstract
A 23-kDa serine protease was partially purified (1800-fold) from the cytosolic fraction of transformed C3H/10T1/2 cells. The purification procedure included chromatography with diethylaminoethyl (DEAE)-Sephacel, BBI-Sepharose, and C18 reverse phase high performance liquid chromatography (HPLC). The partially purified protease had a pH optimum of 7.8 for the hydrolysis of the synthetic tetrapeptide succinyl-Ala-Ala-Pro-Phe-AFC (Km= 0.27 mM). The protease showed no other hydrolyzing activity against a number of various protease-specific synthetic peptides. The protease was inhibited by a number of serine protease inhibitors including Bowman-Birk inhibitor (BBI) (Ki= 0.7 nM) and chymostatin (Ki= 20 nM).
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