title: Purification and characterization of aminopeptidase activity from rat urine.
abstract: The aminopeptidase activity of rat urine was tested using L-aminoacyl-2-naphthylamides and L-Leu-p-nitroanilide. The enzyme preparation was purified by ion-exchange and gel filtration chromatography and showed only a single 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 Ki for amino acids, antibiotics and anti-inflammatory drugs).
authors.affiliation: Departamento de Bioquímica, Escola Paulista de Medicina, São Paulo, Brasil.
authors.forename: K B
authors.initials: KB
authors.lastname: Alves
authors.forename: M A
authors.initials: MA
authors.lastname: Noguti
authors.forename: M M
authors.initials: MM
authors.lastname: Silva
authors.forename: C M
authors.initials: CM
authors.lastname: Brandi
mesh_terms: D000626:Aminopeptidases / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism* / Q000652:urine*; D000818:Animals; D002413:Cations, Divalent / Q000494:pharmacology; D007700:Kinetics; D051381:Rats
chemical_list: D002413:Cations, Divalent; D000626:Aminopeptidases