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...

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Veröffentlicht in:	Biochemical and biophysical research communications 1987-10, Vol.148 (1), p.24-30
Hauptverfasser:	VAEROY, H, NYBERG, F, FRANZEN, H, TERENIUS, L
Format:	Artikel
Sprache:	eng
Schlagworte:	Applied sciences Chromatography, High Pressure Liquid Chromatography, Ion Exchange Ditiocarb - pharmacology Exact sciences and technology Humans Kinetics Mixed Function Oxygenases Multienzyme Complexes Nervous System Diseases - cerebrospinal fluid Nervous System Diseases - enzymology Other techniques and industries Oxidoreductases Acting on CH-NH Group Donors - cerebrospinal fluid Oxidoreductases Acting on CH-NH Group Donors - isolation & purification Protein Processing, Post-Translational
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Zusammenfassung:	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.
ISSN:	0006-291X 1090-2104
DOI:	10.1016/0006-291X(87)91071-0