Effects of ethylenic bond position upon acyltransferase activity with isomeric cis-octadecenoyl coenzyme a thiol esters
dc.contributor.author | Reitz, Ronald C. | en_US |
dc.contributor.author | El-Sheikh, Mustafa | en_US |
dc.contributor.author | Lands, William E. M. | en_US |
dc.contributor.author | Ismail, I. A. | en_US |
dc.contributor.author | Gunstone, Frank D. | en_US |
dc.date.accessioned | 2006-04-17T15:20:42Z | |
dc.date.available | 2006-04-17T15:20:42Z | |
dc.date.issued | 1969-04-29 | en_US |
dc.identifier.citation | Reitz, Ronald C., El-Sheikh, Mustafa, Lands, William E. M., Ismail, I. A., Gunstone, Frank D. (1969/04/29)."Effects of ethylenic bond position upon acyltransferase activity with isomeric cis-octadecenoyl coenzyme a thiol esters." Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism 176(3): 480-490. <http://hdl.handle.net/2027.42/32981> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6T1X-47G2SNK-N2/2/a4a0a877b8248be980ae4fde4c09c681 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/32981 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=5800039&dopt=citation | en_US |
dc.description.abstract | The specificity of the acyl-CoA:phospholipid acyltransferases has been studied using the 16 positional isomers of cis-octadecenoic acid. The results showed that the acyl-transferases acting at both the 1- and 2-positions of acyl-glycero-3-phosphorylcholine (acyl-GPC) discriminated between the acyl-CoA isomers in quite different ways. 1. 1. Acyl-CoA:1-acyl-GPC acyltransferase activity showed a distinct preference for the 9-, and 12-isomers. Of these three, the 9-octadecenoate (oleate) was the preferred substrate having a rate of 98 nmoles/min per mg.2. 2. Acyl-CoA:2-acyl-GPC acyltransferase reacted more rapidly with the 8-,10-,12-,13- and 15-isomers, and of these the 12-octadecenoate had the fastest rate (121 nmoles/min per mg).3. 3. As the enzymes were allowed to age at 4[deg], the activity was lost at slightly different rates for each isomer. The enzyme(s) esterifying the 1-position seemed to loose activity fairly uniformly with all isomers so that a similar pattern of reactivities was observed over a period of several days. The enzyme(s) esterifying the 2-position, however, differed in that after 2 days, the rate for the 9-isomer had dropped below that for the 12-isomer. This result suggests that different enzymes may exist for different acyl-CoA isomers.4. 4. High concentrations of sucrose (0.8 M) tended to stabilize the activities with the 9- and 12-isomers, but did not change the fact that the activity for the 9-isomer was lost more rapidly. Albumin, contrary to our expectations, increased the rate of loss of activity.5. 5. The enzyme activities were purified 10- to 15-fold above that of the crude tissue homogenate by treating the microsomal particles with sodium deoxycholate and albumin.6. 6. Acyltransferase rates for the esterification of the naturally occurring 7-,9-,11-, and 13-octadecenoates to position 1 and 2 of diacyl-GPC indicated a preferred position for each acid which is in accord with that reported for the distribution of these monoenoic acids in phospholipids isolated from rat liver. | en_US |
dc.format.extent | 1075232 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 | Effects of ethylenic bond position upon acyltransferase activity with isomeric cis-octadecenoyl coenzyme a thiol esters | 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 | University of Michigan, Department of Biological Chemistry, Ann Arbor, Mich. 48104, U.S.A. | en_US |
dc.contributor.affiliationum | University of Michigan, Department of Biological Chemistry, Ann Arbor, Mich. 48104, U.S.A. | en_US |
dc.contributor.affiliationum | University of Michigan, Department of Biological Chemistry, Ann Arbor, Mich. 48104, U.S.A. | en_US |
dc.contributor.affiliationum | University of Michigan, Department of Biological Chemistry, Ann Arbor, Mich. 48104, U.S.A. | en_US |
dc.contributor.affiliationother | Chemistry Department, St. Salvator's College, University of St. Andrews, St. Andrews, Great Britain | en_US |
dc.identifier.pmid | 5800039 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/32981/1/0000365.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0005-2760(69)90215-X | en_US |
dc.identifier.source | Biochimica et Biophysica Acta | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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