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The effect of acyl-group composition on the rate of acyltransferase-catalyzed synthesis of lecithin

dc.contributor.authorBrandt, Alan E.en_US
dc.contributor.authorLands, William E. M.en_US
dc.date.accessioned2006-04-17T15:32:39Z
dc.date.available2006-04-17T15:32:39Z
dc.date.issued1967-12-05en_US
dc.identifier.citationBrandt, Alan E., Lands, W. E. M. (1967/12/05)."The effect of acyl-group composition on the rate of acyltransferase-catalyzed synthesis of lecithin." Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism 144(3): 605-612. <http://hdl.handle.net/2027.42/33249>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6T1X-47F71T7-HJ/2/d8c459ea43ac8ff6d0d517a78769e055en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/33249
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=5624813&dopt=citationen_US
dc.description.abstractThe acyltransferase rates for 66 combinations of substrates (6 acylglycerolphosphorylcholines and II acylcoenzyme A derivatives) were measured using an enzyme preparation from pig liver. The results support the earlier findings with ratliver enzymes showing that the position to be acylated was more significant than the composition of fatty acids in the I-acylglycerolphosphorylcholine.en_US
dc.format.extent764244 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.titleThe effect of acyl-group composition on the rate of acyltransferase-catalyzed synthesis of lecithinen_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, The University of Michigan, Ann Arbor, Mich., U.S.A.en_US
dc.contributor.affiliationumDepartment of Biological Chemistry, The University of Michigan, Ann Arbor, Mich., U.S.A.en_US
dc.identifier.pmid5624813en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/33249/1/0000641.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0005-2760(67)90049-5en_US
dc.identifier.sourceBiochimica et Biophysica Actaen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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