dc.contributor.author | Berkhout, Theo | |
dc.contributor.author | Groot, P. H. | |
dc.contributor.author | van Belzen, R. | |
dc.contributor.author | Wirtz, K. W. | |
dc.date.accessioned | 2014-06-11T09:00:33Z | |
dc.date.available | 2014-06-11T09:00:33Z | |
dc.date.issued | 1985-08 | |
dc.identifier.citation | Berkhout , 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.issn | 0022-2275 | |
dc.identifier.uri | http://hdl.handle.net/2299/13689 | |
dc.description.abstract | High 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.extent | 6 | |
dc.language.iso | eng | |
dc.relation.ispartof | Journal of Lipid Research | |
dc.subject | Affinity Labels | |
dc.subject | Apolipoprotein A-I | |
dc.subject | Apolipoprotein A-II | |
dc.subject | Apolipoproteins A | |
dc.subject | Glycolipids | |
dc.subject | Humans | |
dc.subject | Lipoproteins, HDL | |
dc.subject | Macromolecular Substances | |
dc.subject | Molecular Conformation | |
dc.subject | Photochemistry | |
dc.title | Coupling of photoactivatable glycolipid probes to apolipoproteins A-I and A-II in human high density lipoproteins 2 and 3 | en |
dc.contributor.institution | School of Life and Medical Sciences | |
dc.contributor.institution | Department of Pharmacy | |
dc.contributor.institution | Health & Human Sciences Research Institute | |
dc.contributor.institution | Medicinal and Analytical Chemistry | |
dc.description.status | Peer reviewed | |
rioxxterms.type | Journal Article/Review | |
herts.preservation.rarelyaccessed | true | |