Spectrophotometric assay for superoxide dismutase based on the reduction of highly water-soluble tetrazolium salts by xanthine-xanthine oxidase
Two novel highly water-soluble tetrazolium salts, WST-1 (4-[3-(4-iodophenyl)-2-(4-nitrophenyl)-2H-5-tetrazolio]-1,3-benzene disulfonate sodium salt) and WST-8 (4-[3-(2-methoxy-4-nitrophenyl)-2-(4-nitrophenyl)-2 H-5-tetrazolio]-1,3-benzene disulfonate sodium salt) were applied to the assay of superox...
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| Veröffentlicht in: | Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 1999-01, Vol.63 (3), p.485-488 |
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| container_title | Bioscience, biotechnology, and biochemistry |
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| creator | Ukeda, H. (Kochi Univ., Nankoku (Japan). Faculty of Agriculture) Kawana, D Maeda, S Sawamura, M |
| description | Two novel highly water-soluble tetrazolium salts, WST-1 (4-[3-(4-iodophenyl)-2-(4-nitrophenyl)-2H-5-tetrazolio]-1,3-benzene disulfonate sodium salt) and WST-8 (4-[3-(2-methoxy-4-nitrophenyl)-2-(4-nitrophenyl)-2 H-5-tetrazolio]-1,3-benzene disulfonate sodium salt) were applied to the assay of superoxide dismutase (SOD). The superoxide anion generated by xanthine/xanthine oxidase (XO) reduced WST-1 and WST-S to water-soluble formazans which exhibited absorbance maxima at 438 and 460 nm, respectively. The rates of reduction were linearly related to the XO activity, and reduction was inhibited by SOD. Complete inhibition by SOD of the reduction of both WST-1 and WST-8 was achieved, suggesting that these WSTs were not reduced with XO. WST-1 was found more useful than WST-8 because it had shown higher sensitivity which was apparently not dependent on the assay pH value in the range pH 8.0-10.2. These properties of WST-1 are ideal for the spectrophotometric assay of SOD in an aqueous syst |
| doi_str_mv | 10.1271/bbb.63.485 |
| format | Article |
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(Kochi Univ., Nankoku (Japan). Faculty of Agriculture) ; Kawana, D ; Maeda, S ; Sawamura, M</creator><creatorcontrib>Ukeda, H. (Kochi Univ., Nankoku (Japan). Faculty of Agriculture) ; Kawana, D ; Maeda, S ; Sawamura, M</creatorcontrib><description>Two novel highly water-soluble tetrazolium salts, WST-1 (4-[3-(4-iodophenyl)-2-(4-nitrophenyl)-2H-5-tetrazolio]-1,3-benzene disulfonate sodium salt) and WST-8 (4-[3-(2-methoxy-4-nitrophenyl)-2-(4-nitrophenyl)-2 H-5-tetrazolio]-1,3-benzene disulfonate sodium salt) were applied to the assay of superoxide dismutase (SOD). The superoxide anion generated by xanthine/xanthine oxidase (XO) reduced WST-1 and WST-S to water-soluble formazans which exhibited absorbance maxima at 438 and 460 nm, respectively. The rates of reduction were linearly related to the XO activity, and reduction was inhibited by SOD. Complete inhibition by SOD of the reduction of both WST-1 and WST-8 was achieved, suggesting that these WSTs were not reduced with XO. WST-1 was found more useful than WST-8 because it had shown higher sensitivity which was apparently not dependent on the assay pH value in the range pH 8.0-10.2. These properties of WST-1 are ideal for the spectrophotometric assay of SOD in an aqueous syst</description><identifier>ISSN: 0916-8451</identifier><identifier>EISSN: 1347-6947</identifier><identifier>DOI: 10.1271/bbb.63.485</identifier><identifier>PMID: 27393255</identifier><language>eng</language><publisher>Tokyo: Japan Society for Bioscience, Biotechnology, and Agrochemistry</publisher><subject>Analytical, structural and metabolic biochemistry ; assay ; Biological and medical sciences ; Enzymes and enzyme inhibitors ; ESPECTROMETRIA ; Fundamental and applied biological sciences. Psychology ; Oxidoreductases ; SPECTROMETRIE ; SPECTROMETRY ; SUPEROXIDE DISMUTASE ; SUPEROXIDO DISMUTASA ; SUPEROXYDE DISMUTASE ; water-soluble tetrazolium ; WST ; XANTHINE OXIDASE ; XANTHINE OXYDASE ; XANTINA OXIDASA</subject><ispartof>Bioscience, biotechnology, and biochemistry, 1999-01, Vol.63 (3), p.485-488</ispartof><rights>1999 by Japan Society for Bioscience, Biotechnology, and Agrochemistry 1999</rights><rights>1999 INIST-CNRS</rights><rights>Copyright Japan Science and Technology Agency 1999</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c602t-89422fcf7a66487419831fcf3270bcabeebb6cfce6df7eb2d638e02d36568d3f3</citedby><cites>FETCH-LOGICAL-c602t-89422fcf7a66487419831fcf3270bcabeebb6cfce6df7eb2d638e02d36568d3f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1899319$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27393255$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ukeda, H. (Kochi Univ., Nankoku (Japan). Faculty of Agriculture)</creatorcontrib><creatorcontrib>Kawana, D</creatorcontrib><creatorcontrib>Maeda, S</creatorcontrib><creatorcontrib>Sawamura, M</creatorcontrib><title>Spectrophotometric assay for superoxide dismutase based on the reduction of highly water-soluble tetrazolium salts by xanthine-xanthine oxidase</title><title>Bioscience, biotechnology, and biochemistry</title><addtitle>Biosci Biotechnol Biochem</addtitle><description>Two novel highly water-soluble tetrazolium salts, WST-1 (4-[3-(4-iodophenyl)-2-(4-nitrophenyl)-2H-5-tetrazolio]-1,3-benzene disulfonate sodium salt) and WST-8 (4-[3-(2-methoxy-4-nitrophenyl)-2-(4-nitrophenyl)-2 H-5-tetrazolio]-1,3-benzene disulfonate sodium salt) were applied to the assay of superoxide dismutase (SOD). The superoxide anion generated by xanthine/xanthine oxidase (XO) reduced WST-1 and WST-S to water-soluble formazans which exhibited absorbance maxima at 438 and 460 nm, respectively. The rates of reduction were linearly related to the XO activity, and reduction was inhibited by SOD. Complete inhibition by SOD of the reduction of both WST-1 and WST-8 was achieved, suggesting that these WSTs were not reduced with XO. WST-1 was found more useful than WST-8 because it had shown higher sensitivity which was apparently not dependent on the assay pH value in the range pH 8.0-10.2. These properties of WST-1 are ideal for the spectrophotometric assay of SOD in an aqueous syst</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>assay</subject><subject>Biological and medical sciences</subject><subject>Enzymes and enzyme inhibitors</subject><subject>ESPECTROMETRIA</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Oxidoreductases</subject><subject>SPECTROMETRIE</subject><subject>SPECTROMETRY</subject><subject>SUPEROXIDE DISMUTASE</subject><subject>SUPEROXIDO DISMUTASA</subject><subject>SUPEROXYDE DISMUTASE</subject><subject>water-soluble tetrazolium</subject><subject>WST</subject><subject>XANTHINE OXIDASE</subject><subject>XANTHINE OXYDASE</subject><subject>XANTINA OXIDASA</subject><issn>0916-8451</issn><issn>1347-6947</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><recordid>eNptkUFrFDEUxwdR7Fq9eFcCehBh1mSSSSbHUmxVCgrqOSSZl25KZrImGdr1S_iVTdldBfGS5IXf-78Hv6Z5TvCadIK8M8asOV2zoX_QrAhlouWSiYfNCkvC24H15KR5kvMNxvWjJ4-bk05QSbu-XzW_vm7BlhS3m1jiBCV5i3TOeodcTCgvW0jxzo-ARp-npegMyNRjRHFGZQMowbjY4msVHdr4603YoVtdILU5hsUEQKWG6p8x-GVCWYeSkdmhOz2XjZ-hPT7Q_ZQa_LR55HTI8OxwnzbfL95_O__QXn2-_Hh-dtVajrvSDpJ1nbNOaM7ZIBiRAyW1pp3AxmoDYAy3zgIfnQDTjZwOgLuR8p4PI3X0tHmzz92m-GOBXNTks4UQ9AxxyYoMmDImRE8q-uof9CYuaa7bKcKYZLQXhFfq7Z6yKeacwKlt8pNOO0WwutekqibFqaqaKvzyELmYCcY_6NFLBV4fAJ2tDi7p2fr8N3KQkhJZsX6P-bnqmvRtTGFURe9CTMce-t_5L_Z9Tkelr1PFPn0hUkqM-UAo_Q0v9LmA</recordid><startdate>19990101</startdate><enddate>19990101</enddate><creator>Ukeda, H. (Kochi Univ., Nankoku (Japan). Faculty of Agriculture)</creator><creator>Kawana, D</creator><creator>Maeda, S</creator><creator>Sawamura, M</creator><general>Japan Society for Bioscience, Biotechnology, and Agrochemistry</general><general>Japan Society for Bioscience Biotechnology and Agrochemistry</general><general>Oxford University Press</general><scope>FBQ</scope><scope>IQODW</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19990101</creationdate><title>Spectrophotometric assay for superoxide dismutase based on the reduction of highly water-soluble tetrazolium salts by xanthine-xanthine oxidase</title><author>Ukeda, H. (Kochi Univ., Nankoku (Japan). Faculty of Agriculture) ; Kawana, D ; Maeda, S ; Sawamura, M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c602t-89422fcf7a66487419831fcf3270bcabeebb6cfce6df7eb2d638e02d36568d3f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>assay</topic><topic>Biological and medical sciences</topic><topic>Enzymes and enzyme inhibitors</topic><topic>ESPECTROMETRIA</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Oxidoreductases</topic><topic>SPECTROMETRIE</topic><topic>SPECTROMETRY</topic><topic>SUPEROXIDE DISMUTASE</topic><topic>SUPEROXIDO DISMUTASA</topic><topic>SUPEROXYDE DISMUTASE</topic><topic>water-soluble tetrazolium</topic><topic>WST</topic><topic>XANTHINE OXIDASE</topic><topic>XANTHINE OXYDASE</topic><topic>XANTINA OXIDASA</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ukeda, H. (Kochi Univ., Nankoku (Japan). Faculty of Agriculture)</creatorcontrib><creatorcontrib>Kawana, D</creatorcontrib><creatorcontrib>Maeda, S</creatorcontrib><creatorcontrib>Sawamura, M</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Bioscience, biotechnology, and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ukeda, H. (Kochi Univ., Nankoku (Japan). 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The superoxide anion generated by xanthine/xanthine oxidase (XO) reduced WST-1 and WST-S to water-soluble formazans which exhibited absorbance maxima at 438 and 460 nm, respectively. The rates of reduction were linearly related to the XO activity, and reduction was inhibited by SOD. Complete inhibition by SOD of the reduction of both WST-1 and WST-8 was achieved, suggesting that these WSTs were not reduced with XO. WST-1 was found more useful than WST-8 because it had shown higher sensitivity which was apparently not dependent on the assay pH value in the range pH 8.0-10.2. These properties of WST-1 are ideal for the spectrophotometric assay of SOD in an aqueous syst</abstract><cop>Tokyo</cop><pub>Japan Society for Bioscience, Biotechnology, and Agrochemistry</pub><pmid>27393255</pmid><doi>10.1271/bbb.63.485</doi><tpages>4</tpages></addata></record> |
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| ispartof | Bioscience, biotechnology, and biochemistry, 1999-01, Vol.63 (3), p.485-488 |
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| recordid | cdi_pascalfrancis_primary_1899319 |
| source | J-STAGE Free; Oxford University Press Journals All Titles (1996-Current); Freely Accessible Japanese Titles; EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry |
| subjects | Analytical, structural and metabolic biochemistry assay Biological and medical sciences Enzymes and enzyme inhibitors ESPECTROMETRIA Fundamental and applied biological sciences. Psychology Oxidoreductases SPECTROMETRIE SPECTROMETRY SUPEROXIDE DISMUTASE SUPEROXIDO DISMUTASA SUPEROXYDE DISMUTASE water-soluble tetrazolium WST XANTHINE OXIDASE XANTHINE OXYDASE XANTINA OXIDASA |
| title | Spectrophotometric assay for superoxide dismutase based on the reduction of highly water-soluble tetrazolium salts by xanthine-xanthine oxidase |
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