Abstract
1. 1. SH-protease inhibitor was purified from newborn rat epidermis and its activity against cathepsins B and H compared using α-N- benzoyl- dl-arginine -2- napthylamide as a substrate. 2. 2. Preincubation of the inhibitor with the enzymes at 37°C resulted in increased inhibitor activity for cathepsin B but not for cathepsin H: pH 7.0 was more effective than the lower pH for the increase. 3. 3. The inhibition was noncompetitive regardless of the preincubation conditions and the inhibition was greater for cathepsin H than cathepsin B. 4. 4. These findings suggest that there is an SH-protease inhibitor of newborn rat epidermis which has different biological behavior against cathepsins B and H.
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