The role of superoxide and singlet oxygen in lipid peroxidation promoted by xanthine oxidase
The peroxidative oxidation of extracted rat liver microsomal lipid, assayed as malondialdehyde production, can be promoted by milk xanthine oxidase in the presence of 0.2 mM FeCl 3 and 0.1 mM EDTA. The reaction is inhibited by the superoxide dismutase activity of erythrocuprein. The reaction is also...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1973-01, Vol.52 (3), p.1071-1078 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Pederson, T.C. Aust, S.D. |
| description | The peroxidative oxidation of extracted rat liver microsomal lipid, assayed as malondialdehyde production, can be promoted by milk xanthine oxidase in the presence of 0.2 mM FeCl
3 and 0.1 mM EDTA. The reaction is inhibited by the superoxide dismutase activity of erythrocuprein. The reaction is also inhibited by 1,3-diphenylisobenzofuran, which reacts with singlet oxygen to yield dibenzoylbenzene. During inhibition of the lipid peroxidation reaction by 1,3-diphenylisobenzofuran, o-dibenzoylbenzene was produced. The rate of superoxide production by xanthine oxidase was not affected by 1,3-diphenylisobenzofuran. Lipid peroxidation promoted by ascorbic acid is not inhibited by either erythrocuprein or 1,3-diphenylisobenzofuran. Therefore it is suggested that the peroxidative oxidation of unsaturated lipid promoted by xanthine oxidase involves the formation of singlet oxygen from superoxide, and the singlet oxygen reacts with the lipid to form fatty acid hydroperoxides. |
| doi_str_mv | 10.1016/0006-291X(73)91047-4 |
| format | Article |
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3 and 0.1 mM EDTA. The reaction is inhibited by the superoxide dismutase activity of erythrocuprein. The reaction is also inhibited by 1,3-diphenylisobenzofuran, which reacts with singlet oxygen to yield dibenzoylbenzene. During inhibition of the lipid peroxidation reaction by 1,3-diphenylisobenzofuran, o-dibenzoylbenzene was produced. The rate of superoxide production by xanthine oxidase was not affected by 1,3-diphenylisobenzofuran. Lipid peroxidation promoted by ascorbic acid is not inhibited by either erythrocuprein or 1,3-diphenylisobenzofuran. Therefore it is suggested that the peroxidative oxidation of unsaturated lipid promoted by xanthine oxidase involves the formation of singlet oxygen from superoxide, and the singlet oxygen reacts with the lipid to form fatty acid hydroperoxides.</description><subject>Animals</subject><subject>Benzofurans</subject><subject>Chromatography, Gel</subject><subject>Chromatography, Thin Layer</subject><subject>Copper - analysis</subject><subject>Cytochrome c Group - metabolism</subject><subject>Free Radicals</subject><subject>Lipid Metabolism</subject><subject>Liposomes - metabolism</subject><subject>Microsomes, Liver</subject><subject>Milk - enzymology</subject><subject>Oxidation-Reduction</subject><subject>Oxidoreductases - metabolism</subject><subject>Oxygen</subject><subject>Rats</subject><subject>Spectrophotometry, Atomic</subject><subject>Superoxide Dismutase - metabolism</subject><subject>Xanthine Oxidase - metabolism</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1973</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kF1LwzAUhoMoc378A4VciV5UkzZNlhtBhl8w8GaCF0JIm9Mt0iUzaWX797au7NKrcHif8yZ5ELqg5JYSyu8IITxJJf24FtmNpISJhB2gMSWSJGk3HqLxHjlGJzF-EUIp43KERizLOyIfo8_5EnDwNWBf4diuIfiNNYC1Mzhat6ihwX6zXYDD1uHarq3BA6Qb6x1eB7_yDRhcbPFGu2ZpXdfVxxHO0FGl6wjnw3mK3p8e59OXZPb2_Dp9mCUly9MmYYRXXBe8yAyhYLgWhhCZa2M047oSk1QXYiJYpgXQokN5Riec0rJICykly07R1a63e8x3C7FRKxtLqGvtwLdRTahMieCyA9kOLIOPMUCl1sGudNgqSlQvVfXGVG9MiUz9SVV9_-XQ3xYrMPulwWKX3-9y6D75YyGoWFpwJRgboGyU8fb_C34BjaiHhQ</recordid><startdate>19730101</startdate><enddate>19730101</enddate><creator>Pederson, T.C.</creator><creator>Aust, S.D.</creator><general>Elsevier Inc</general><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>19730101</creationdate><title>The role of superoxide and singlet oxygen in lipid peroxidation promoted by xanthine oxidase</title><author>Pederson, T.C. ; Aust, S.D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c452t-406f6ab6b3d01ed6a7d0095adda46af782ab78743a7e1bf6a6318611cb2b99943</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1973</creationdate><topic>Animals</topic><topic>Benzofurans</topic><topic>Chromatography, Gel</topic><topic>Chromatography, Thin Layer</topic><topic>Copper - analysis</topic><topic>Cytochrome c Group - metabolism</topic><topic>Free Radicals</topic><topic>Lipid Metabolism</topic><topic>Liposomes - metabolism</topic><topic>Microsomes, Liver</topic><topic>Milk - enzymology</topic><topic>Oxidation-Reduction</topic><topic>Oxidoreductases - metabolism</topic><topic>Oxygen</topic><topic>Rats</topic><topic>Spectrophotometry, Atomic</topic><topic>Superoxide Dismutase - metabolism</topic><topic>Xanthine Oxidase - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pederson, T.C.</creatorcontrib><creatorcontrib>Aust, S.D.</creatorcontrib><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>Pederson, T.C.</au><au>Aust, S.D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The role of superoxide and singlet oxygen in lipid peroxidation promoted by xanthine oxidase</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1973-01-01</date><risdate>1973</risdate><volume>52</volume><issue>3</issue><spage>1071</spage><epage>1078</epage><pages>1071-1078</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>The peroxidative oxidation of extracted rat liver microsomal lipid, assayed as malondialdehyde production, can be promoted by milk xanthine oxidase in the presence of 0.2 mM FeCl
3 and 0.1 mM EDTA. The reaction is inhibited by the superoxide dismutase activity of erythrocuprein. The reaction is also inhibited by 1,3-diphenylisobenzofuran, which reacts with singlet oxygen to yield dibenzoylbenzene. During inhibition of the lipid peroxidation reaction by 1,3-diphenylisobenzofuran, o-dibenzoylbenzene was produced. The rate of superoxide production by xanthine oxidase was not affected by 1,3-diphenylisobenzofuran. Lipid peroxidation promoted by ascorbic acid is not inhibited by either erythrocuprein or 1,3-diphenylisobenzofuran. Therefore it is suggested that the peroxidative oxidation of unsaturated lipid promoted by xanthine oxidase involves the formation of singlet oxygen from superoxide, and the singlet oxygen reacts with the lipid to form fatty acid hydroperoxides.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>4351045</pmid><doi>10.1016/0006-291X(73)91047-4</doi><tpages>8</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 1973-01, Vol.52 (3), p.1071-1078 |
| issn | 0006-291X 1090-2104 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Animals Benzofurans Chromatography, Gel Chromatography, Thin Layer Copper - analysis Cytochrome c Group - metabolism Free Radicals Lipid Metabolism Liposomes - metabolism Microsomes, Liver Milk - enzymology Oxidation-Reduction Oxidoreductases - metabolism Oxygen Rats Spectrophotometry, Atomic Superoxide Dismutase - metabolism Xanthine Oxidase - metabolism |
| title | The role of superoxide and singlet oxygen in lipid peroxidation promoted by xanthine oxidase |
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