HPLC-based bioactivity profiling of plant extracts: a kinetic assay for the identification of monoamine oxidase-A inhibitors using human recombinant monoamine oxidase-A

An assay for the HPLC-based search for monoamine oxidase-A inhibitors in plant extracts is reported. The applicability to HPLC-based activity profiling is tested with plant extracts spiked with small amounts of known MAO inhibitors. An assay for the HPLC-based search for monoamine oxidase-A (MAO-A)...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Phytochemistry (Oxford) 2004-11, Vol.65 (21), p.2885-2891
Hauptverfasser: Dittmann, Kathrin, Riese, Ulrike, Hamburger, Matthias
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 2891
container_issue 21
container_start_page 2885
container_title Phytochemistry (Oxford)
container_volume 65
creator Dittmann, Kathrin
Riese, Ulrike
Hamburger, Matthias
description An assay for the HPLC-based search for monoamine oxidase-A inhibitors in plant extracts is reported. The applicability to HPLC-based activity profiling is tested with plant extracts spiked with small amounts of known MAO inhibitors. An assay for the HPLC-based search for monoamine oxidase-A (MAO-A) inhibitors in plant extracts was established. It combines human recombinant MAO-A, expressed as GST-fusion protein in yeast, with a kinetic measurement of the conversion of kynuramine to 4-hydroxyquinoline. Substrate selectivity and kinetic parameters of the GST-fusion protein were comparable to the wild-type enzyme. The applicability of the assay to HPLC-based activity profiling was tested with plant extracts spiked with small amounts of known MAO inhibitors.
doi_str_mv 10.1016/j.phytochem.2004.07.024
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_67003593</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0031942204003887</els_id><sourcerecordid>67003593</sourcerecordid><originalsourceid>FETCH-LOGICAL-c423t-b51c8b2d2984df3ed1b51bec0b3c900ea166ca6526d72c5be10e6b4eccd854ac3</originalsourceid><addsrcrecordid>eNqFkc1uEzEUhUcIREPhFag3sJtw7ZnxJOyiqLRIkUCCri3_3GluyNjBdqrmjXjMOkpEN0isRvJ8x8c6X1VdcZhy4PLTZrpbH3KwaxynAqCdQj8F0b6oJnzWN3XTA7ysJgANr-etEBfVm5Q2ANB1Ur6uLnjXARednFR_br-vlrXRCR0zFLTN9ED5wHYxDLQlf8_CwHZb7TPDxxzL__SZafaLPGayTKekD2wIkeU1MnLoMw1kdabgj8kx-KDHArPwSK601AtGfk2GcoiJ7dOxYb0ftWcRbRgN-WPVP2Jvq1eD3iZ8d_5eVndfrn8ub-vVt5uvy8Wqtq1ocm06bmdGODGftW5o0PFyYtCCaewcADWX0mrZCel6YTuDHFCaFq11s67VtrmsPp7uLQv83mPKaqRkcVsmwLBPSpZpm27eFLA_gTaGlCIOahdp1PGgOKijJLVRfyWpoyQFvSqSSvL9uWJvRnTPubOVAnw4AzpZvR2i9pbSMyeF6HroC3d14gYdlL6Phbn7IYA3AHNZXPNCLE4ElskeCKNKltBbdFT2zsoF-u9znwB9e8J5</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>67003593</pqid></control><display><type>article</type><title>HPLC-based bioactivity profiling of plant extracts: a kinetic assay for the identification of monoamine oxidase-A inhibitors using human recombinant monoamine oxidase-A</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Dittmann, Kathrin ; Riese, Ulrike ; Hamburger, Matthias</creator><creatorcontrib>Dittmann, Kathrin ; Riese, Ulrike ; Hamburger, Matthias</creatorcontrib><description>An assay for the HPLC-based search for monoamine oxidase-A inhibitors in plant extracts is reported. The applicability to HPLC-based activity profiling is tested with plant extracts spiked with small amounts of known MAO inhibitors. An assay for the HPLC-based search for monoamine oxidase-A (MAO-A) inhibitors in plant extracts was established. It combines human recombinant MAO-A, expressed as GST-fusion protein in yeast, with a kinetic measurement of the conversion of kynuramine to 4-hydroxyquinoline. Substrate selectivity and kinetic parameters of the GST-fusion protein were comparable to the wild-type enzyme. The applicability of the assay to HPLC-based activity profiling was tested with plant extracts spiked with small amounts of known MAO inhibitors.</description><identifier>ISSN: 0031-9422</identifier><identifier>EISSN: 1873-3700</identifier><identifier>DOI: 10.1016/j.phytochem.2004.07.024</identifier><identifier>PMID: 15501256</identifier><language>eng</language><publisher>Amsterdam: Elsevier Ltd</publisher><subject>Activity profiling ; amine oxidase (flavin-containing) ; Biological and medical sciences ; Chemical constitution ; Chromatography, High Pressure Liquid ; enzyme inhibitors ; enzyme kinetics ; Fundamental and applied biological sciences. Psychology ; gene expression ; GST-fusion protein ; high performance liquid chromatography ; HPLC ; Human recombinant ; Humans ; Kinetics ; Lead discovery ; molecular sequence data ; Monoamine Oxidase - metabolism ; Monoamine oxidase A ; Monoamine Oxidase Inhibitors - pharmacology ; nucleotide sequences ; phytochemicals ; Plant extract ; plant extracts ; Plant Extracts - chemistry ; Plant Extracts - pharmacology ; Plant physiology and development ; recombinant fusion proteins ; Recombinant Proteins - metabolism ; Reproducibility of Results ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - metabolism ; Sensitivity and Specificity ; Substrate Specificity</subject><ispartof>Phytochemistry (Oxford), 2004-11, Vol.65 (21), p.2885-2891</ispartof><rights>2004 Elsevier Ltd</rights><rights>2004 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c423t-b51c8b2d2984df3ed1b51bec0b3c900ea166ca6526d72c5be10e6b4eccd854ac3</citedby><cites>FETCH-LOGICAL-c423t-b51c8b2d2984df3ed1b51bec0b3c900ea166ca6526d72c5be10e6b4eccd854ac3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0031942204003887$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=16225707$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15501256$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dittmann, Kathrin</creatorcontrib><creatorcontrib>Riese, Ulrike</creatorcontrib><creatorcontrib>Hamburger, Matthias</creatorcontrib><title>HPLC-based bioactivity profiling of plant extracts: a kinetic assay for the identification of monoamine oxidase-A inhibitors using human recombinant monoamine oxidase-A</title><title>Phytochemistry (Oxford)</title><addtitle>Phytochemistry</addtitle><description>An assay for the HPLC-based search for monoamine oxidase-A inhibitors in plant extracts is reported. The applicability to HPLC-based activity profiling is tested with plant extracts spiked with small amounts of known MAO inhibitors. An assay for the HPLC-based search for monoamine oxidase-A (MAO-A) inhibitors in plant extracts was established. It combines human recombinant MAO-A, expressed as GST-fusion protein in yeast, with a kinetic measurement of the conversion of kynuramine to 4-hydroxyquinoline. Substrate selectivity and kinetic parameters of the GST-fusion protein were comparable to the wild-type enzyme. The applicability of the assay to HPLC-based activity profiling was tested with plant extracts spiked with small amounts of known MAO inhibitors.</description><subject>Activity profiling</subject><subject>amine oxidase (flavin-containing)</subject><subject>Biological and medical sciences</subject><subject>Chemical constitution</subject><subject>Chromatography, High Pressure Liquid</subject><subject>enzyme inhibitors</subject><subject>enzyme kinetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>gene expression</subject><subject>GST-fusion protein</subject><subject>high performance liquid chromatography</subject><subject>HPLC</subject><subject>Human recombinant</subject><subject>Humans</subject><subject>Kinetics</subject><subject>Lead discovery</subject><subject>molecular sequence data</subject><subject>Monoamine Oxidase - metabolism</subject><subject>Monoamine oxidase A</subject><subject>Monoamine Oxidase Inhibitors - pharmacology</subject><subject>nucleotide sequences</subject><subject>phytochemicals</subject><subject>Plant extract</subject><subject>plant extracts</subject><subject>Plant Extracts - chemistry</subject><subject>Plant Extracts - pharmacology</subject><subject>Plant physiology and development</subject><subject>recombinant fusion proteins</subject><subject>Recombinant Proteins - metabolism</subject><subject>Reproducibility of Results</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Sensitivity and Specificity</subject><subject>Substrate Specificity</subject><issn>0031-9422</issn><issn>1873-3700</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1uEzEUhUcIREPhFag3sJtw7ZnxJOyiqLRIkUCCri3_3GluyNjBdqrmjXjMOkpEN0isRvJ8x8c6X1VdcZhy4PLTZrpbH3KwaxynAqCdQj8F0b6oJnzWN3XTA7ysJgANr-etEBfVm5Q2ANB1Ur6uLnjXARednFR_br-vlrXRCR0zFLTN9ED5wHYxDLQlf8_CwHZb7TPDxxzL__SZafaLPGayTKekD2wIkeU1MnLoMw1kdabgj8kx-KDHArPwSK601AtGfk2GcoiJ7dOxYb0ftWcRbRgN-WPVP2Jvq1eD3iZ8d_5eVndfrn8ub-vVt5uvy8Wqtq1ocm06bmdGODGftW5o0PFyYtCCaewcADWX0mrZCel6YTuDHFCaFq11s67VtrmsPp7uLQv83mPKaqRkcVsmwLBPSpZpm27eFLA_gTaGlCIOahdp1PGgOKijJLVRfyWpoyQFvSqSSvL9uWJvRnTPubOVAnw4AzpZvR2i9pbSMyeF6HroC3d14gYdlL6Phbn7IYA3AHNZXPNCLE4ElskeCKNKltBbdFT2zsoF-u9znwB9e8J5</recordid><startdate>20041101</startdate><enddate>20041101</enddate><creator>Dittmann, Kathrin</creator><creator>Riese, Ulrike</creator><creator>Hamburger, Matthias</creator><general>Elsevier Ltd</general><general>Elsevier</general><scope>FBQ</scope><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>20041101</creationdate><title>HPLC-based bioactivity profiling of plant extracts: a kinetic assay for the identification of monoamine oxidase-A inhibitors using human recombinant monoamine oxidase-A</title><author>Dittmann, Kathrin ; Riese, Ulrike ; Hamburger, Matthias</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c423t-b51c8b2d2984df3ed1b51bec0b3c900ea166ca6526d72c5be10e6b4eccd854ac3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Activity profiling</topic><topic>amine oxidase (flavin-containing)</topic><topic>Biological and medical sciences</topic><topic>Chemical constitution</topic><topic>Chromatography, High Pressure Liquid</topic><topic>enzyme inhibitors</topic><topic>enzyme kinetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>gene expression</topic><topic>GST-fusion protein</topic><topic>high performance liquid chromatography</topic><topic>HPLC</topic><topic>Human recombinant</topic><topic>Humans</topic><topic>Kinetics</topic><topic>Lead discovery</topic><topic>molecular sequence data</topic><topic>Monoamine Oxidase - metabolism</topic><topic>Monoamine oxidase A</topic><topic>Monoamine Oxidase Inhibitors - pharmacology</topic><topic>nucleotide sequences</topic><topic>phytochemicals</topic><topic>Plant extract</topic><topic>plant extracts</topic><topic>Plant Extracts - chemistry</topic><topic>Plant Extracts - pharmacology</topic><topic>Plant physiology and development</topic><topic>recombinant fusion proteins</topic><topic>Recombinant Proteins - metabolism</topic><topic>Reproducibility of Results</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Sensitivity and Specificity</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dittmann, Kathrin</creatorcontrib><creatorcontrib>Riese, Ulrike</creatorcontrib><creatorcontrib>Hamburger, Matthias</creatorcontrib><collection>AGRIS</collection><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>Phytochemistry (Oxford)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dittmann, Kathrin</au><au>Riese, Ulrike</au><au>Hamburger, Matthias</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>HPLC-based bioactivity profiling of plant extracts: a kinetic assay for the identification of monoamine oxidase-A inhibitors using human recombinant monoamine oxidase-A</atitle><jtitle>Phytochemistry (Oxford)</jtitle><addtitle>Phytochemistry</addtitle><date>2004-11-01</date><risdate>2004</risdate><volume>65</volume><issue>21</issue><spage>2885</spage><epage>2891</epage><pages>2885-2891</pages><issn>0031-9422</issn><eissn>1873-3700</eissn><abstract>An assay for the HPLC-based search for monoamine oxidase-A inhibitors in plant extracts is reported. The applicability to HPLC-based activity profiling is tested with plant extracts spiked with small amounts of known MAO inhibitors. An assay for the HPLC-based search for monoamine oxidase-A (MAO-A) inhibitors in plant extracts was established. It combines human recombinant MAO-A, expressed as GST-fusion protein in yeast, with a kinetic measurement of the conversion of kynuramine to 4-hydroxyquinoline. Substrate selectivity and kinetic parameters of the GST-fusion protein were comparable to the wild-type enzyme. The applicability of the assay to HPLC-based activity profiling was tested with plant extracts spiked with small amounts of known MAO inhibitors.</abstract><cop>Amsterdam</cop><pub>Elsevier Ltd</pub><pmid>15501256</pmid><doi>10.1016/j.phytochem.2004.07.024</doi><tpages>7</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0031-9422
ispartof Phytochemistry (Oxford), 2004-11, Vol.65 (21), p.2885-2891
issn 0031-9422
1873-3700
language eng
recordid cdi_proquest_miscellaneous_67003593
source MEDLINE; Elsevier ScienceDirect Journals
subjects Activity profiling
amine oxidase (flavin-containing)
Biological and medical sciences
Chemical constitution
Chromatography, High Pressure Liquid
enzyme inhibitors
enzyme kinetics
Fundamental and applied biological sciences. Psychology
gene expression
GST-fusion protein
high performance liquid chromatography
HPLC
Human recombinant
Humans
Kinetics
Lead discovery
molecular sequence data
Monoamine Oxidase - metabolism
Monoamine oxidase A
Monoamine Oxidase Inhibitors - pharmacology
nucleotide sequences
phytochemicals
Plant extract
plant extracts
Plant Extracts - chemistry
Plant Extracts - pharmacology
Plant physiology and development
recombinant fusion proteins
Recombinant Proteins - metabolism
Reproducibility of Results
Saccharomyces cerevisiae
Saccharomyces cerevisiae - metabolism
Sensitivity and Specificity
Substrate Specificity
title HPLC-based bioactivity profiling of plant extracts: a kinetic assay for the identification of monoamine oxidase-A inhibitors using human recombinant monoamine oxidase-A
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-26T13%3A33%3A21IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=HPLC-based%20bioactivity%20profiling%20of%20plant%20extracts:%20a%20kinetic%20assay%20for%20the%20identification%20of%20monoamine%20oxidase-A%20inhibitors%20using%20human%20recombinant%20monoamine%20oxidase-A&rft.jtitle=Phytochemistry%20(Oxford)&rft.au=Dittmann,%20Kathrin&rft.date=2004-11-01&rft.volume=65&rft.issue=21&rft.spage=2885&rft.epage=2891&rft.pages=2885-2891&rft.issn=0031-9422&rft.eissn=1873-3700&rft_id=info:doi/10.1016/j.phytochem.2004.07.024&rft_dat=%3Cproquest_cross%3E67003593%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=67003593&rft_id=info:pmid/15501256&rft_els_id=S0031942204003887&rfr_iscdi=true