Fractionation of the rat liver enzymes that hydrolyze benzoyl-arginine-2-naphthylamide.
1. The enzyme activity in the particulate fraction from rat liver that hydrolyzes alpha-N-benzoyl-DL-arginine-2-naphthylamide (Bz-Arg-NNap) has been separated into two approximately equal components by chromatography on DEAE-cellulose. One component (peak II) is completely retained by the column at low ionic strength while the other component (peak I) passes through. 2. In contrast to the enzyme in peak I, the enzyme in peak II is extremely sensitive to inhibition by leupeptin, it will hydrolyze carbobenzoxy-alanylarginylarginyl-4-methoxy-2-naphthylamine, and it will inactivate aldolase. 3. There appears to be also a minor high molecular weight component of the alpha-N-benzoyl-DL-arginyl-2-naphthylamine-hydrolyzing activity that is retained by the DEAE-cellulose but which has properties similar to those of the peak I enzyme.
D000818:Animals; D001587:Benzoylarginine-2-Naphthylamide; D002848:Chromatography, DEAE-Cellulose; D005260:Female; D007700:Kinetics; D007976:Leupeptins / Q000494:pharmacology; D008099:Liver / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D051381:Rats
D007976:Leupeptins; D001587:Benzoylarginine-2-Naphthylamide; D010447:Peptide Hydrolases