Differences in the behavior of SH-protease inhibitor of rat epidermis on cathepsins B and H.
1. SH-protease inhibitor was purified from newborn rat epidermis and its activity against cathepsins B and H compared using alpha-N-benzoyl-DL-arginine-2-napthylamide as a substrate. 2. Preincubation of the inhibitor with the enzymes at 37 degrees 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. The inhibition was noncompetitive regardless of the preincubation conditions and the inhibition was greater for cathepsin H than cathepsin B. 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.
D000818:Animals; D002401:Cathepsin B; D056655:Cathepsin H; D002403:Cathepsins / Q000378:metabolism*; D003546:Cysteine Endopeptidases; D004817:Epidermis / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D011480:Protease Inhibitors / Q000494:pharmacology*; D051381:Rats; D011919:Rats, Inbred Strains; D013696:Temperature
D011480:Protease Inhibitors; D002403:Cathepsins; D003546:Cysteine Endopeptidases; D002401:Cathepsin B; D056655:Cathepsin H; C534128:Ctsh protein, rat