Preparation of 1-acyl-2-succinyl glycero-3-phosphorylcholine and evidence against its involvement in succinate dehydrogenase action
1-Acyl-2-succinyl glycero-3-phosphorylcholine (GPC) was synthesized and its properties described. Although 1-acyl-2-succinyl GPC is a good substrate for succinate dehydrogenase, experiments on the incorporation of [2,3- 14C]succinate into mitochondrial lipids gave no evidence to indicate that it is...
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| Veröffentlicht in: | Chemistry and physics of lipids 1976-11, Vol.17 (4), p.407-415 |
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| container_issue | 4 |
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| container_title | Chemistry and physics of lipids |
| container_volume | 17 |
| creator | Brain, F.H. Davison, A.N. Natarjan, V. Sastry, P.S. |
| description | 1-Acyl-2-succinyl glycero-3-phosphorylcholine (GPC) was synthesized and its properties described. Although 1-acyl-2-succinyl GPC is a good substrate for succinate dehydrogenase, experiments on the incorporation of [2,3-
14C]succinate into mitochondrial lipids gave no evidence to indicate that it is an intermediate in the enzymic oxidation of succinate to fumarate, as has been suggested earlier. |
| doi_str_mv | 10.1016/0009-3084(76)90042-6 |
| format | Article |
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14C]succinate into mitochondrial lipids gave no evidence to indicate that it is an intermediate in the enzymic oxidation of succinate to fumarate, as has been suggested earlier.</description><subject>Animals</subject><subject>Cyanides - pharmacology</subject><subject>Glycerylphosphorylcholine - analogs & derivatives</subject><subject>Lysophosphatidylcholines</subject><subject>Microsomes, Liver - drug effects</subject><subject>Microsomes, Liver - enzymology</subject><subject>Mitochondria, Liver - drug effects</subject><subject>Mitochondria, Liver - enzymology</subject><subject>Phospholipases</subject><subject>Rats</subject><subject>Snake Venoms</subject><subject>Succinate Dehydrogenase - metabolism</subject><issn>0009-3084</issn><issn>1873-2941</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1976</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEFv3CAQhVHUpN2k_Qc5cKraAykYmzWXStEqTSutlBxyRxiGXSoWtuC15HP-eO04yjGH0ehp3nuID6FrRm8YZeIHpVQSTtv621p8l5TWFRFnaMXaNSeVrNkHtHqzfEKXpfydJG0a9hFdSMm4pCv0_JjhqLPufYo4OcyINmMgFSknY3wcA96F0UBOhJPjPpVp8hjMPgUfAetoMQzeQjST2GkfS499X7CPQwoDHCBOOuKlTPeALexHm9MOoi5TxMzvfkbnTocCX173FXr6dfe0-U22D_d_NrdbYngjelKxGjprwTbGMaapa6kznXN1ZxoQEhptRSc5AwmcOd5qU7edZA54xyvb8iv0dak95vTvBKVXB18MhKAjpFNRLW_aWtDZWC9Gk1MpGZw6Zn_QeVSMqpm8mrGqGataC_VCXokpdv3af-oOYN9CC-rp_HM5w_TFwUNWxfgZnPUZTK9s8u_3_wdympaI</recordid><startdate>197611</startdate><enddate>197611</enddate><creator>Brain, F.H.</creator><creator>Davison, A.N.</creator><creator>Natarjan, V.</creator><creator>Sastry, P.S.</creator><general>Elsevier Ireland Ltd</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>197611</creationdate><title>Preparation of 1-acyl-2-succinyl glycero-3-phosphorylcholine and evidence against its involvement in succinate dehydrogenase action</title><author>Brain, F.H. ; Davison, A.N. ; Natarjan, V. ; Sastry, P.S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c356t-214ebdded5cf11a0f80fcbff4bc5e69e5ad6b931e9e31f38ac48b91fe3b32d83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1976</creationdate><topic>Animals</topic><topic>Cyanides - pharmacology</topic><topic>Glycerylphosphorylcholine - analogs & derivatives</topic><topic>Lysophosphatidylcholines</topic><topic>Microsomes, Liver - drug effects</topic><topic>Microsomes, Liver - enzymology</topic><topic>Mitochondria, Liver - drug effects</topic><topic>Mitochondria, Liver - enzymology</topic><topic>Phospholipases</topic><topic>Rats</topic><topic>Snake Venoms</topic><topic>Succinate Dehydrogenase - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Brain, F.H.</creatorcontrib><creatorcontrib>Davison, A.N.</creatorcontrib><creatorcontrib>Natarjan, V.</creatorcontrib><creatorcontrib>Sastry, P.S.</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>Chemistry and physics of lipids</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Brain, F.H.</au><au>Davison, A.N.</au><au>Natarjan, V.</au><au>Sastry, P.S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Preparation of 1-acyl-2-succinyl glycero-3-phosphorylcholine and evidence against its involvement in succinate dehydrogenase action</atitle><jtitle>Chemistry and physics of lipids</jtitle><addtitle>Chem Phys Lipids</addtitle><date>1976-11</date><risdate>1976</risdate><volume>17</volume><issue>4</issue><spage>407</spage><epage>415</epage><pages>407-415</pages><issn>0009-3084</issn><eissn>1873-2941</eissn><abstract>1-Acyl-2-succinyl glycero-3-phosphorylcholine (GPC) was synthesized and its properties described. Although 1-acyl-2-succinyl GPC is a good substrate for succinate dehydrogenase, experiments on the incorporation of [2,3-
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| identifier | ISSN: 0009-3084 |
| ispartof | Chemistry and physics of lipids, 1976-11, Vol.17 (4), p.407-415 |
| issn | 0009-3084 1873-2941 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Animals Cyanides - pharmacology Glycerylphosphorylcholine - analogs & derivatives Lysophosphatidylcholines Microsomes, Liver - drug effects Microsomes, Liver - enzymology Mitochondria, Liver - drug effects Mitochondria, Liver - enzymology Phospholipases Rats Snake Venoms Succinate Dehydrogenase - metabolism |
| title | Preparation of 1-acyl-2-succinyl glycero-3-phosphorylcholine and evidence against its involvement in succinate dehydrogenase action |
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