Separation of enkephalin-degrading enzymes from longitudinal muscle layer of bovine small intestine. Enzyme inhibition by arphamenine A.
The enkephalin-degrading enzymes, such as aminopeptidase, dipeptidyl aminopeptidase, dipeptidyl carboxypeptidase and carboxypeptidase, were purified partially by DEAE-cellulose column chromatography, using longitudinal muscle from bovine small intestine. These enzyme were inhibited by EDTA and o-phenanthroline. Several protease inhibitors of microbial origin, and synthetic compounds, were tested for their abilities to inhibit these enkephalin-degrading enzymes. Among them, arphamenine A, a new potent inhibitor for aminopeptidase B, was shown to be a useful compound in inhibiting all of the enkephalin-degrading enzymes in small intestine.
D000626:Aminopeptidases / Q000037:antagonists & inhibitors / Q000302:isolation & purification; D000818:Animals; D001345:Autoradiography; D002268:Carboxypeptidases / Q000037:antagonists & inhibitors / Q000302:isolation & purification; D002417:Cattle; D002848:Chromatography, DEAE-Cellulose; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / Q000037:antagonists & inhibitors / Q000302:isolation & purification; D010450:Endopeptidases / Q000302:isolation & purification; D004745:Enkephalins / Q000378:metabolism*; D006146:Guanidines / Q000494:pharmacology*; D007421:Intestine, Small / Q000201:enzymology*; D009130:Muscle, Smooth / Q000201:enzymology*; D010446:Peptide Fragments / Q000032:analysis; D011480:Protease Inhibitors
D004745:Enkephalins; D006146:Guanidines; D010446:Peptide Fragments; D011480:Protease Inhibitors; C040038:arphamenine A; D002268:Carboxypeptidases; D010450:Endopeptidases; D000626:Aminopeptidases; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; C020071:dipeptidyl carboxypeptidase