1999 Volume 5 Issue 2 Pages 210-213
An intracellular cysteine protease inhibitor (ICPI) from Chlorella sp. was purified to homogeneity judging from polyacrylamide gel electrophoresis. The purified inhibitor had a molecular mass of 410kDa and a pI of 5.3. ICPI retained 100% of the original activity even after heating at 100°C for 5 min. It exhibited an inhibitory activity against the proteolytic activity of papain, ficin, chymopapain, calcium dependent neutral protease and bromelain, but not against cathepsin B, pepsin, trypsin, or α-chymotrypsin. The inhibitory activity was inactivated by α-chymotrypsin. ICPI contained 76% carbohydrate residues by weight and inhibited papain at a ratio of 1:3. From these results, we assume that ICPI is a novel type of cysteine protease inhibitor.