Metabolism of plasmalogen III. Relative reactivities of acyl and alkenyl derivatives of glycerol-3-phosphorylcholine
dc.contributor.author | Lands, William E. M. | en_US |
dc.contributor.author | Hart, Priscilla | en_US |
dc.date.accessioned | 2006-04-13T14:42:34Z | |
dc.date.available | 2006-04-13T14:42:34Z | |
dc.date.issued | 1965-06-01 | en_US |
dc.identifier.citation | Lands, William E. M., Hart, Priscilla (1965/06/01)."Metabolism of plasmalogen III. Relative reactivities of acyl and alkenyl derivatives of glycerol-3-phosphorylcholine." Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism 98(3): 532-538. <http://hdl.handle.net/2027.42/32018> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6T1X-47GJ086-B/2/c83c449a99927969dc7118c4e2daba0c | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/32018 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=5837453&dopt=citation | en_US |
dc.description.abstract | 1. (1) The alkenyl ether derivatives of phospholipids (plasmalogens) react at slower rates than the acyl analogs in several enzyme-catalyzed reactions.2. (2) Alkenylglycerol-3-phosphorylcholine is essentially inert as a substrate for acyl-CoA: phospholipid acyltransf erase. This result suggests that in vivo the 2-acyl substituent may be present before the alkenyl ether group is formed in the molecule.3. (3) Alkenyl acylglycerol 3-phosphorylcholine is essentially inert as a substrate for cabbage phospholipase D (EC 3.1.4.4.). This lack of reactivity allows a convenient separation of alkenyl acylglycerol 3-phosphorylcholine from its diacyl analog in naturally occurring mixtures. | en_US |
dc.format.extent | 473590 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Metabolism of plasmalogen III. Relative reactivities of acyl and alkenyl derivatives of glycerol-3-phosphorylcholine | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Materials Science and Engineering | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, University of Michigan, Ann Arbor, Mich, U.S.A. | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, University of Michigan, Ann Arbor, Mich, U.S.A. | en_US |
dc.identifier.pmid | 5837453 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/32018/1/0000060.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0005-2760(65)90149-9 | en_US |
dc.identifier.source | Biochimica et Biophysica Acta | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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