title: Characterization of a substance P-Gly12 amidating enzyme in human cerebrospinal fluid.
abstract: Enzyme activity capable of converting the glycine-extended substance P precursor, substance P-Gly12, into substance P was purified from human cerebrospinal fluid. The conversion reaction was monitored by radioimmunoassay measurement of substance P formation. The chemical identity of the product was verified by reversed-phase HPLC. The enzyme reaction was stimulated by Cu(II) ion and ascorbic acid and inhibited by the presence of diethyldithiocarbamate. By HPLC molecular sieving, the major enzyme activity appeared as a protein of 26,000 molecular weight.
authors.affiliation: Department of Pharmacology, University of Uppsala, Sweden.
authors.forename: H
authors.initials: H
authors.lastname: Vaeröy
authors.forename: F
authors.initials: F
authors.lastname: Nyberg
authors.forename: H
authors.initials: H
authors.lastname: Franzén
authors.forename: L
authors.initials: L
authors.lastname: Terenius
mesh_terms: D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004050:Ditiocarb / Q000494:pharmacology; D006801:Humans; D007700:Kinetics; D006899:Mixed Function Oxygenases; D009097:Multienzyme Complexes; D009422:Nervous System Diseases / Q000134:cerebrospinal fluid / Q000201:enzymology; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000134:cerebrospinal fluid* / Q000302:isolation & purification; D011499:Protein Processing, Post-Translational
chemical_list: D009097:Multienzyme Complexes; D004050:Ditiocarb; D006899:Mixed Function Oxygenases; C035189:peptidylglycine monooxygenase; D000587:Oxidoreductases Acting on CH-NH Group Donors