CHARACTERIZATION OF ENZYMES HYDROLYZING ACYL NAPHTHYLAMIDES: I. MONO-AND DIHALOGEN DERIVATIVES

Abstract

A biochemical amid histochemical investigation of the enzymes miied!iating the hyd!rolysis of monoand !ihalogen acyl na )hthylamides in the kidneys of several species revealed that these enzymes were separable from those hydrolyzing L-leucyl and a-L-glutalflyl -naphthylamides and N-acvl anuiinoacids (acvlase 1), but not fromim several hvd!rolyzing acet inilide, amino and Nacyl amino acid ester’s, and arviesters. Inhibition by typical esterase inhibitors indicated that these acylan’ylami(!e-hydrolyzing enzymes had esterolvtic activity. It was determined that the enzymes hvdrolvzing the acylai’ylanmide substrates were found in highest proportion in the soluble fraction of kidney homogenates and were inhibited by d!iazoniunii salts, an inhibition influenced by the diazoniumn salt concentration and the pH of the