title: Studies on ox brain aminopeptidases.
abstract: 1. Mn(2+)-inhibited and Mn(2+)-activated aminopeptidases have been observed in ox brain and separated from one another by DEAE-cellulose column chromatography. 2. The Mn(2+)-inhibited enzyme has been purified 36-fold; it exhibits a specificity for tripeptide substrates, whereas the Mn(2+)-activated aminopeptidase cleaves dipeptides as well as tripeptides. 3. Ammonium sulphate treatment generates a Mn(2+)-stimulated aminopeptidase that is stable to dialysis against EDTA and water, in contrast with an endogenous Mn(2+)-activated preparation that is irreversibly denatured by such dialysis against EDTA and water.
mesh_terms: D000626:Aminopeptidases; D000818:Animals; D001921:Brain / Q000201:enzymology*; D002417:Cattle; D002482:Cellulose; D002498:Centrifugation; D002852:Chromatography, Ion Exchange; D003956:Dialysis; D004355:Drug Stability; D004492:Edetic Acid; D008345:Manganese; D010455:Peptides; D011489:Protein Denaturation; D012965:Sodium Chloride; D014325:Tromethamine
chemical_list: D010455:Peptides; D014325:Tromethamine; D008345:Manganese; D012965:Sodium Chloride; D002482:Cellulose; D004492:Edetic Acid; D000626:Aminopeptidases