Differences in the antioxidant mechanism of carnosine in the presence of copper and iron
Carnosine is a beta-alanylhistidine dipeptide found in skeletal muscle. Carnosine (1.0-25 mM) is capable of inhibiting copper- and iron-catalyzed oxidation of phosphatidylcholine liposomes as measured by thiobarbituric acid reactive substances (TBARS) and lipid peroxides. The ability of 5 mM carnosi...
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| Veröffentlicht in: | Journal of agricultural and food chemistry 1992-05, Vol.40 (5), p.756-759 |
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| container_title | Journal of agricultural and food chemistry |
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| creator | Decker, Eric A Crum, Andrea D Calvert, John T |
| description | Carnosine is a beta-alanylhistidine dipeptide found in skeletal muscle. Carnosine (1.0-25 mM) is capable of inhibiting copper- and iron-catalyzed oxidation of phosphatidylcholine liposomes as measured by thiobarbituric acid reactive substances (TBARS) and lipid peroxides. The ability of 5 mM carnosine to inhibit the formation of TBARS and lipid peroxides was 2.5- and 8.8-fold higher, respectively, for copper- than iron-catalyzed lipid oxidation. Carnosine (0.05-10.0 mM) is capable of inhibiting copper-catalyzed oxidation of ascorbic acid but was ineffective at preventing iron-catalyzed ascorbate oxidation. Carnosine inhibits iron-dependent microsomal lipid oxidation but does not inhibit the oxidation of NADPH by the enzyme system. 1H NMR spectra of carnosine show peak broadening in the presence of copper but not iron. These data suggest that carnosine forms a complex with copper which decreases its catalytic activity; however, carnosine does not form a complex with iron |
| doi_str_mv | 10.1021/jf00017a009 |
| format | Article |
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Carnosine (1.0-25 mM) is capable of inhibiting copper- and iron-catalyzed oxidation of phosphatidylcholine liposomes as measured by thiobarbituric acid reactive substances (TBARS) and lipid peroxides. The ability of 5 mM carnosine to inhibit the formation of TBARS and lipid peroxides was 2.5- and 8.8-fold higher, respectively, for copper- than iron-catalyzed lipid oxidation. Carnosine (0.05-10.0 mM) is capable of inhibiting copper-catalyzed oxidation of ascorbic acid but was ineffective at preventing iron-catalyzed ascorbate oxidation. Carnosine inhibits iron-dependent microsomal lipid oxidation but does not inhibit the oxidation of NADPH by the enzyme system. 1H NMR spectra of carnosine show peak broadening in the presence of copper but not iron. These data suggest that carnosine forms a complex with copper which decreases its catalytic activity; however, carnosine does not form a complex with iron</description><identifier>ISSN: 0021-8561</identifier><identifier>EISSN: 1520-5118</identifier><identifier>DOI: 10.1021/jf00017a009</identifier><identifier>CODEN: JAFCAU</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>ANTIOXIDANTES ; ANTIOXYDANT ; Biological and medical sciences ; CATION ; CATIONES ; COBRE ; CUIVRE ; ESPECTROMETRIA ; FER ; Food additives ; Food industries ; Fundamental and applied biological sciences. Psychology ; General aspects ; HIERRO ; INHIBICION ; INHIBITION ; LIPIDE ; LIPIDOS ; METAL ; METALES ; OXIDACION ; OXYDATION ; PEPTIDE ; PEPTIDOS ; SPECTROMETRIE</subject><ispartof>Journal of agricultural and food chemistry, 1992-05, Vol.40 (5), p.756-759</ispartof><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a417t-625e0428d9366be429113a70dfad687e50d2b6e036047d2492ff1c6adc23c14c3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/jf00017a009$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/jf00017a009$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,777,781,2752,27057,27905,27906,56719,56769</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4460315$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Decker, Eric A</creatorcontrib><creatorcontrib>Crum, Andrea D</creatorcontrib><creatorcontrib>Calvert, John T</creatorcontrib><title>Differences in the antioxidant mechanism of carnosine in the presence of copper and iron</title><title>Journal of agricultural and food chemistry</title><addtitle>J. Agric. Food Chem</addtitle><description>Carnosine is a beta-alanylhistidine dipeptide found in skeletal muscle. Carnosine (1.0-25 mM) is capable of inhibiting copper- and iron-catalyzed oxidation of phosphatidylcholine liposomes as measured by thiobarbituric acid reactive substances (TBARS) and lipid peroxides. The ability of 5 mM carnosine to inhibit the formation of TBARS and lipid peroxides was 2.5- and 8.8-fold higher, respectively, for copper- than iron-catalyzed lipid oxidation. Carnosine (0.05-10.0 mM) is capable of inhibiting copper-catalyzed oxidation of ascorbic acid but was ineffective at preventing iron-catalyzed ascorbate oxidation. Carnosine inhibits iron-dependent microsomal lipid oxidation but does not inhibit the oxidation of NADPH by the enzyme system. 1H NMR spectra of carnosine show peak broadening in the presence of copper but not iron. These data suggest that carnosine forms a complex with copper which decreases its catalytic activity; however, carnosine does not form a complex with iron</description><subject>ANTIOXIDANTES</subject><subject>ANTIOXYDANT</subject><subject>Biological and medical sciences</subject><subject>CATION</subject><subject>CATIONES</subject><subject>COBRE</subject><subject>CUIVRE</subject><subject>ESPECTROMETRIA</subject><subject>FER</subject><subject>Food additives</subject><subject>Food industries</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General aspects</subject><subject>HIERRO</subject><subject>INHIBICION</subject><subject>INHIBITION</subject><subject>LIPIDE</subject><subject>LIPIDOS</subject><subject>METAL</subject><subject>METALES</subject><subject>OXIDACION</subject><subject>OXYDATION</subject><subject>PEPTIDE</subject><subject>PEPTIDOS</subject><subject>SPECTROMETRIE</subject><issn>0021-8561</issn><issn>1520-5118</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><recordid>eNptkDtPHDEUha2ISFmWVOlSTYFEEQ3c69fMlAgSHlopoAUlnXXx2OCF9YzsjUT-PSYDKAXVLb7vHF0dxr4g7CNwPFh5AMCGALoPbIaKQ60Q2y02g4LrVmn8xLZzXhWtVQ3M2O_j4L1LLlqXqxCrzZ2rKG7C8Bj6cqu1s3cUQ15Xg68spTjkEN2rOSaXn6P_4DCOLpVwX4U0xB320dNDdp9f7pxd__h-dXRaL36enB0dLmqS2GxqzZUDydu-E1rfOMk7REEN9J563TZOQc9vtAOhQTY9lx33Hq2m3nJhUVoxZ9-mXpuGnJPzZkxhTemvQTDPo5j_Rin27mSPlC09-ETRhvwWkVKDQFW0etJC3rjHN0zp3uhGNMpcXSzN-YlUl4vTX2ZZ_K-T72kwdJtK5fWyEwIl6gL3Jkg2m9XwJ8Wyx7vfPQHjuYSr</recordid><startdate>19920501</startdate><enddate>19920501</enddate><creator>Decker, Eric A</creator><creator>Crum, Andrea D</creator><creator>Calvert, John T</creator><general>American Chemical Society</general><scope>FBQ</scope><scope>BSCLL</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>19920501</creationdate><title>Differences in the antioxidant mechanism of carnosine in the presence of copper and iron</title><author>Decker, Eric A ; Crum, Andrea D ; Calvert, John T</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a417t-625e0428d9366be429113a70dfad687e50d2b6e036047d2492ff1c6adc23c14c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>ANTIOXIDANTES</topic><topic>ANTIOXYDANT</topic><topic>Biological and medical sciences</topic><topic>CATION</topic><topic>CATIONES</topic><topic>COBRE</topic><topic>CUIVRE</topic><topic>ESPECTROMETRIA</topic><topic>FER</topic><topic>Food additives</topic><topic>Food industries</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>General aspects</topic><topic>HIERRO</topic><topic>INHIBICION</topic><topic>INHIBITION</topic><topic>LIPIDE</topic><topic>LIPIDOS</topic><topic>METAL</topic><topic>METALES</topic><topic>OXIDACION</topic><topic>OXYDATION</topic><topic>PEPTIDE</topic><topic>PEPTIDOS</topic><topic>SPECTROMETRIE</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Decker, Eric A</creatorcontrib><creatorcontrib>Crum, Andrea D</creatorcontrib><creatorcontrib>Calvert, John T</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><jtitle>Journal of agricultural and food chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Decker, Eric A</au><au>Crum, Andrea D</au><au>Calvert, John T</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Differences in the antioxidant mechanism of carnosine in the presence of copper and iron</atitle><jtitle>Journal of agricultural and food chemistry</jtitle><addtitle>J. Agric. Food Chem</addtitle><date>1992-05-01</date><risdate>1992</risdate><volume>40</volume><issue>5</issue><spage>756</spage><epage>759</epage><pages>756-759</pages><issn>0021-8561</issn><eissn>1520-5118</eissn><coden>JAFCAU</coden><abstract>Carnosine is a beta-alanylhistidine dipeptide found in skeletal muscle. Carnosine (1.0-25 mM) is capable of inhibiting copper- and iron-catalyzed oxidation of phosphatidylcholine liposomes as measured by thiobarbituric acid reactive substances (TBARS) and lipid peroxides. The ability of 5 mM carnosine to inhibit the formation of TBARS and lipid peroxides was 2.5- and 8.8-fold higher, respectively, for copper- than iron-catalyzed lipid oxidation. Carnosine (0.05-10.0 mM) is capable of inhibiting copper-catalyzed oxidation of ascorbic acid but was ineffective at preventing iron-catalyzed ascorbate oxidation. Carnosine inhibits iron-dependent microsomal lipid oxidation but does not inhibit the oxidation of NADPH by the enzyme system. 1H NMR spectra of carnosine show peak broadening in the presence of copper but not iron. These data suggest that carnosine forms a complex with copper which decreases its catalytic activity; however, carnosine does not form a complex with iron</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><doi>10.1021/jf00017a009</doi><tpages>4</tpages></addata></record> |
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| ispartof | Journal of agricultural and food chemistry, 1992-05, Vol.40 (5), p.756-759 |
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| source | ACS Publications |
| subjects | ANTIOXIDANTES ANTIOXYDANT Biological and medical sciences CATION CATIONES COBRE CUIVRE ESPECTROMETRIA FER Food additives Food industries Fundamental and applied biological sciences. Psychology General aspects HIERRO INHIBICION INHIBITION LIPIDE LIPIDOS METAL METALES OXIDACION OXYDATION PEPTIDE PEPTIDOS SPECTROMETRIE |
| title | Differences in the antioxidant mechanism of carnosine in the presence of copper and iron |
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