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 |
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| container_title | Biochemical and biophysical research communications |
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| creator | VAEROY, H NYBERG, F FRANZEN, H TERENIUS, L |
| description | 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. |
| doi_str_mv | 10.1016/0006-291X(87)91071-0 |
| format | Article |
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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. 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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.</description><subject>Applied sciences</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Chromatography, Ion Exchange</subject><subject>Ditiocarb - pharmacology</subject><subject>Exact sciences and technology</subject><subject>Humans</subject><subject>Kinetics</subject><subject>Mixed Function Oxygenases</subject><subject>Multienzyme Complexes</subject><subject>Nervous System Diseases - cerebrospinal fluid</subject><subject>Nervous System Diseases - enzymology</subject><subject>Other techniques and industries</subject><subject>Oxidoreductases Acting on CH-NH Group Donors - cerebrospinal fluid</subject><subject>Oxidoreductases Acting on CH-NH Group Donors - isolation & purification</subject><subject>Protein Processing, Post-Translational</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kEtLAzEUhYMotVb_gUIWIroYvTeZR2YpRatQ0IUFdyGTZDQyj5rMLNpf79QOXd3F-c7h8hFyiXCPgOkDAKQRy_HzVmR3OUKGERyRKUIOEUOIj8n0gJySsxB-ABDjNJ-QCROMC4inZDX_Vl7pznq3VZ1rG9qWVNHQF6FTjbb0PVpUG2RU1c4MQPNFbbPd1Ja6hn73tWqott4Wvg1r16iKllXvzDk5KVUV7MV4Z2T1_PQxf4mWb4vX-eMy0izlXcS4TjXYQrMkFiWmWOYaCqZzSOKCJywGkRSmYJBoBcYYldkSUbPcamNQIJ-Rm_3u2re_vQ2drF3QtqpUY9s-SIEIXOTJAMZ7UA-PBm9LufauVn4jEeTOptypkjtVUmTy36aEoXY17vdFbc2hNOob8usxV0GrqvSDMhcOWCbijKec_wEzcH0Q</recordid><startdate>19871014</startdate><enddate>19871014</enddate><creator>VAEROY, H</creator><creator>NYBERG, F</creator><creator>FRANZEN, H</creator><creator>TERENIUS, L</creator><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19871014</creationdate><title>Characterization of a substance P-Gly12 amidating enzyme in human cerebrospinal fluid</title><author>VAEROY, H ; NYBERG, F ; FRANZEN, H ; TERENIUS, L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c263t-23c6c0ebc2548f161f9c0b2c9054b3524085bdb205ca0ddda7ef11c29ecdd1813</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Applied sciences</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Chromatography, Ion Exchange</topic><topic>Ditiocarb - pharmacology</topic><topic>Exact sciences and technology</topic><topic>Humans</topic><topic>Kinetics</topic><topic>Mixed Function Oxygenases</topic><topic>Multienzyme Complexes</topic><topic>Nervous System Diseases - cerebrospinal fluid</topic><topic>Nervous System Diseases - enzymology</topic><topic>Other techniques and industries</topic><topic>Oxidoreductases Acting on CH-NH Group Donors - cerebrospinal fluid</topic><topic>Oxidoreductases Acting on CH-NH Group Donors - isolation & purification</topic><topic>Protein Processing, Post-Translational</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>VAEROY, H</creatorcontrib><creatorcontrib>NYBERG, F</creatorcontrib><creatorcontrib>FRANZEN, H</creatorcontrib><creatorcontrib>TERENIUS, L</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>VAEROY, H</au><au>NYBERG, F</au><au>FRANZEN, H</au><au>TERENIUS, L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of a substance P-Gly12 amidating enzyme in human cerebrospinal fluid</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1987-10-14</date><risdate>1987</risdate><volume>148</volume><issue>1</issue><spage>24</spage><epage>30</epage><pages>24-30</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><coden>BBRCA9</coden><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.</abstract><cop>San Diego, CA</cop><pub>Elsevier</pub><pmid>2823804</pmid><doi>10.1016/0006-291X(87)91071-0</doi><tpages>7</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 1987-10, Vol.148 (1), p.24-30 |
| issn | 0006-291X 1090-2104 |
| language | eng |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | 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 |
| title | Characterization of a substance P-Gly12 amidating enzyme in human cerebrospinal fluid |
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