Characterization of a substance P-Gly12 amidating enzyme in human cerebrospinal fluid |
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| Authors: | H Vaer?y F Nyberg H Franzén L Terenius |
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| Institution: | Department of Pharmacology, University of Uppsala, Sweden. |
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| 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. |
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