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dc.contributor.authorBerkhout, Theo
dc.contributor.authorVanamerongen, A.
dc.contributor.authorWirtz, K.W.A.
dc.date.accessioned2014-02-27T10:29:02Z
dc.date.available2014-02-27T10:29:02Z
dc.date.issued1984-07
dc.identifier.citationBerkhout , T , Vanamerongen , A & Wirtz , K W A 1984 , ' Labeling of phospholipids in vesicles and human-erythrocytes by photoactivable fatty-acid derivatives ' , European Journal of Biochemistry , vol. 142 , no. 1 , pp. 91-97 . https://doi.org/10.1111/j.1432-1033.1984.tb08254.x
dc.identifier.issn0014-2956
dc.identifier.urihttp://hdl.handle.net/2299/12934
dc.description.abstractThe photoactivable glycolipid probes, 2-(4-azido-2-nitrophenoxy)palmitoyl[1-I4C]glucosamine (compound A) and 12-(4-azido-2-nitrophenoxy)stearoyl[1-14C]glucosamine (compound B) were synthesized essentially as described before [Iwata, K. K. et al. (1978) Prog. Clin. Biol. Res. 22, 579–589]. These probes were used to label phospholipid vesicles and erythrocyte membranes. A chromatographic method was developed to quantify the individual probe-phospholipid adducts involving both phosphatidylcholine, phosphatidylethanolamine, and phosphatidylserine. For both membranes as well as for both probes a phospholipid labeling pattern was obtained which appeared to reflect the relative content of fatty acid double bonds in each phospholipid class. The distinct labeling of phosphatidylserine in intact erythrocytes strongly suggested that the probes spontaneously and rapidly redistributed between the two halves of the membrane bilayer. In addition, both probes yielded an extensive labeling of the membrane proteins. Analysis by dodecylsulfate-polyacrylamide gel electrophoresis and autoradiography has indicated that the protein labeling pattern was different, depending on whether the ‘shallow’ probe (compound A) or ‘depth’ probe (compound B) were useden
dc.format.extent7
dc.language.isoeng
dc.relation.ispartofEuropean Journal of Biochemistry
dc.titleLabeling of phospholipids in vesicles and human-erythrocytes by photoactivable fatty-acid derivativesen
dc.contributor.institutionDepartment of Pharmacy
dc.contributor.institutionSchool of Life and Medical Sciences
dc.contributor.institutionHealth & Human Sciences Research Institute
dc.contributor.institutionMedicinal and Analytical Chemistry
dc.description.statusPeer reviewed
rioxxterms.versionofrecord10.1111/j.1432-1033.1984.tb08254.x
rioxxterms.typeJournal Article/Review
herts.preservation.rarelyaccessedtrue


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