Alpha-N-benzoylarginine-2-naphthylamide hydrolase (cathepsin B1?) from rat skin. I. Preliminary experiments with skin extract.
The cathepsin B1-like, alpha-N-benzoyl-DL-arginine-2-naphthylamide (BANA) hydrolyzing activity of rat skin extract was studied. The enzyme was extracted into low ionic strength buffers, and was activated by dithiothreitol, EDTA and KCN. Incubation of the extract at acidic pH resulted in a 3.6-fold increase in its BANA hydrolase activity. The presence of inhibitor(s) of BANA hydrolase in the skin extract was indicated by the non-linearity of the activity/enzyme concentration curve and by Sephadex G-100 gel chromatography, which also caused separation of several other skin proteases.
D000818:Animals; D001587:Benzoylarginine-2-Naphthylamide; D002403:Cathepsins / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D002850:Chromatography, Gel; D003486:Cyanides / Q000494:pharmacology; D004229:Dithiothreitol / Q000494:pharmacology; D004492:Edetic Acid / Q000494:pharmacology; D010450:Endopeptidases / Q000302:isolation & purification*; D004789:Enzyme Activation / Q000187:drug effects; D006863:Hydrogen-Ion Concentration; D051381:Rats; D012867:Skin / Q000201:enzymology*; D013268:Stimulation, Chemical; D014020:Tissue Extracts
D003486:Cyanides; D014020:Tissue Extracts; D001587:Benzoylarginine-2-Naphthylamide; D004492:Edetic Acid; D002403:Cathepsins; D010450:Endopeptidases; D004229:Dithiothreitol