Increased activity of a neutral protease in cytosol from rat hepatoma induced by N-2-fluorenylacetamide.
A protease active with N-alpha-benzoyl-DL-arginine-p-nitroanilide with an optimum pH of 7.3 has been found in the cytosol of rat liver. The activity of this protease increased in N-2-fluorenylacetamide-induced hepatoma as well as in fetal liver. It has been purified from normal liver and hepatoma about 200-fold. Its molecular weight is estimated by gel filtration to be about 200,000 in each tissue. The protease activity is unaffected by chymostatin, pepstatin, soybean trypsin inhibitor, and p-chloromercuribenzoate. Antipain, leupeptin, tosyl-L-lysine chloromethyl ketone, and phenylmethylsulfonyl fluoride inhibit the protease activity. This protease appears to be a serine protease.
D015073:2-Acetylaminofluorene; D000818:Animals; D003600:Cytosol / Q000201:enzymology; D007526:Isoelectric Point; D008099:Liver / Q000196:embryology / Q000201:enzymology; D008114:Liver Neoplasms, Experimental / Q000139:chemically induced / Q000378:metabolism*; D008115:Liver Regeneration; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D051381:Rats
D015073:2-Acetylaminofluorene; D010447:Peptide Hydrolases