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dc.contributor.authorBerkhout, Theo
dc.contributor.authorGroot, P. H.
dc.contributor.authorvan Belzen, R.
dc.contributor.authorWirtz, K. W.
dc.date.accessioned2014-06-11T09:00:33Z
dc.date.available2014-06-11T09:00:33Z
dc.date.issued1985-08
dc.identifier.citationBerkhout , T , Groot , P H , van Belzen , R & Wirtz , K W 1985 , ' Coupling of photoactivatable glycolipid probes to apolipoproteins A-I and A-II in human high density lipoproteins 2 and 3 ' , Journal of Lipid Research , vol. 26 , no. 8 , pp. 964-9 .
dc.identifier.issn0022-2275
dc.identifier.otherPURE: 7130996
dc.identifier.otherPURE UUID: 80d1a344-b3e6-4af7-b46c-51c5e349ad2b
dc.identifier.otherPubMed: 3930643
dc.identifier.otherScopus: 0022415858
dc.identifier.urihttp://hdl.handle.net/2299/13689
dc.description.abstractHigh density lipoprotein (HDL) from human serum was subfractionated into HDL2 and HDL3 by rate-zonal density gradient ultracentrifugation. The orientation of apoproteins (apo) A-I and A-II in these subfractions was investigated by use of the photosensitive glycolipid probes, 2-(4-azido-2-nitrophenoxy)-palmitoyl[1-14C]glucosamine (compound A) and 12-(4-azido-2-nitrophenoxy)-stearoyl[1-14C]glucosamine (compound B). Both probes were added to the HDL-structures in a ratio of two or three probe molecules per particle and were photoactivated by irradiation at a wavelength above 340 nm. After delipidation the probe-apoprotein adducts were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Both the "shallow" probe (compound A) and the "depth" probe (compound B) were coupled for 10-14% (of the label added) to apoA-I and apoA-II from HDL3 and for about 6% to apoA-I and apoA-II from HDL2. By taking into account the relative amounts of apoA-I and apoA-II, it was estimated that the "shallow" probe labeled apoA-I 40% more effectively than apoA-II in both HDL2 and HDL3; the "depth" probe labeled apoA-I and apoA-II equally well in both subfractions. The data suggest that towards the surface HDL2 and HDL3 contain a relatively larger portion of apoA-I than apoA-II, whilst towards the core both subfractions are occupied by an equal portion of apoA-I and apoA-II. Application of these photolabels has failed to point out differences in the structural organization of HDL2 and HDL3.en
dc.format.extent6
dc.language.isoeng
dc.relation.ispartofJournal of Lipid Research
dc.subjectAffinity Labels
dc.subjectApolipoprotein A-I
dc.subjectApolipoprotein A-II
dc.subjectApolipoproteins A
dc.subjectGlycolipids
dc.subjectHumans
dc.subjectLipoproteins, HDL
dc.subjectMacromolecular Substances
dc.subjectMolecular Conformation
dc.subjectPhotochemistry
dc.titleCoupling of photoactivatable glycolipid probes to apolipoproteins A-I and A-II in human high density lipoproteins 2 and 3en
dc.contributor.institutionSchool of Life and Medical Sciences
dc.contributor.institutionDepartment of Pharmacy
dc.contributor.institutionHealth & Human Sciences Research Institute
dc.contributor.institutionMedicinal and Analytical Chemistry
dc.description.statusPeer reviewed
dc.relation.schoolSchool of Life and Medical Sciences
dcterms.dateAccepted1985-08
rioxxterms.typeJournal Article/Review
herts.preservation.rarelyaccessedtrue


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