Characterization of a substance P-Gly12 amidating enzyme in human cerebrospinal fluid.
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.
Vaeröy
H
H
Department of Pharmacology, University of Uppsala, Sweden.
Nyberg
F
F
Franzén
H
H
Terenius
L
L
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
D009097:Multienzyme Complexes; D004050:Ditiocarb; D006899:Mixed Function Oxygenases; C035189:peptidylglycine monooxygenase; D000587:Oxidoreductases Acting on CH-NH Group Donors