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Incorporation of ricinoleic acid into glycerolipids
dc.contributor.authorBarber, Eugene D.en_US
dc.contributor.authorSmith, William L.en_US
dc.contributor.authorLands, William E. M.en_US
dc.date.accessioned2006-04-17T16:21:07Z
dc.date.available2006-04-17T16:21:07Z
dc.date.issued1971-11-05en_US
dc.identifier.citationBarber, E. D., Smith, W. L., Lands, W. E. M. (1971/11/05)."Incorporation of ricinoleic acid into glycerolipids." Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism 248(2): 171-179. <http://hdl.handle.net/2027.42/33531>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6T1X-47GH1MT-7P/2/af76c58e259a31589d88580a20f08d6ben_US
dc.identifier.urihttps://hdl.handle.net/2027.42/33531
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=5130450&dopt=citationen_US
dc.description.abstractThe coenzyme A thiol ester of ricinoleic acid was synthesized and characterized. Ricinoleoyl-CoA has been tested as an acyl donor in several in vitro systems using rat liver microsomal acyltransferases.It is essentially inactive when 1-acyl- or 2-acyl-sn-glycerol-3-phosphoryl choline are used as acceptors, however, it can serve as acyl donor when glycerol-3-phosphate or 1-acyl-sn-glycerol-3-phosphate are acceptors to yield di- and monoricinoleoyl glycerol-3-phosphates, respectively. A high apparent Km (50 [mu]M) for ricinoleoyl-CoA may explain the fact that ricinoleic acid appears to be excluded from phospholipids in vivo.en_US
dc.format.extent764437 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleIncorporation of ricinoleic acid into glycerolipidsen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelMaterials Science and Engineeringen_US
dc.subject.hlbsecondlevelChemistryen_US
dc.subject.hlbsecondlevelChemical Engineeringen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelEngineeringen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Biological Chemistry, University of Michigan, Ann Arbor, MI 48104, U.S.A.en_US
dc.contributor.affiliationumDepartment of Biological Chemistry, University of Michigan, Ann Arbor, MI 48104, U.S.A.en_US
dc.contributor.affiliationumDepartment of Biological Chemistry, University of Michigan, Ann Arbor, MI 48104, U.S.A.en_US
dc.identifier.pmid5130450en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/33531/1/0000030.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0005-2760(71)90004-Xen_US
dc.identifier.sourceBiochimica et Biophysica Actaen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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