Purification and characterization of aminopeptidase activity from rat urine

ABSTRACT

The aminopeptidase activity of rats urine was tested using L-aminoacy1-2-naphtylamides and L-Leu-p-nitroanilide. The enzyme preparation was purified by ion-exchange and gel filtration chromatography and showed only a single active protein active protein band on 7.5% polyacrylamide gel electrophoresis. The enzyme was characterized by studying the effects of ions (divalent cations and chloride), chelating agents and -SH and -S-S- group reagents and by determining kinetic parameters (Km and Vmax for different substrates and K1 for amino acids, antibiotics and anti-inflammatory drugs)