title: Purification and properties of a brain enzyme which deiminates proteins.
abstract: The deimination of guanidyl groups of peptides, proteins and other arginine-containing compounds is catalyzed by enzymes found in mammalian brain and epidermis. In cow, the brain and epidermal enzymes differ kinetically and physically, but both may be quantitated by measuring the production of benzoyl citrulline ethyl ester from benzoyl-arginine ethyl ester. The brain enzyme has been purified to apparent homogeneity, as judged by the presence of only one 85,000 dalton band in purified preparations when examined by SDS-polyacrylamide gel electrophoresis. An antibody raised to this band precipitates pure and partially purified brain enzyme but not partially purified epidermal enzyme, using the Ouchterlony technique. The antibody bound to an insoluble matrix removes brain enzyme activity from solution but not epidermal enzyme activity. The Km of the brain enzyme for benzoyl-arginine ethyl ester is about 0.33 mM.
mesh_terms: D000818:Animals; D001921:Brain / Q000201:enzymology*; D002417:Cattle; D006867:Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D051381:Rats; D012867:Skin / Q000201:enzymology; D013045:Species Specificity; D013116:Spinal Cord / Q000201:enzymology; D013379:Substrate Specificity; D014018:Tissue Distribution
chemical_list: D006867:Hydrolases; C019723:arginine deiminase