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dc.contributor.authorWesterman, J.
dc.contributor.authorWirtz, K.W.A.
dc.contributor.authorBerkhout, Theo
dc.contributor.authorVandeenen, L.L.M.
dc.contributor.authorRadhakrishnan, R.
dc.contributor.authorKhorana, H.G.
dc.identifier.citationWesterman , J , Wirtz , K W A , Berkhout , T , Vandeenen , L L M , Radhakrishnan , R & Khorana , H G 1983 , ' Identification of the lipid-binding site of phosphatidylcholine-transfer protein with phosphatidylcholine analogs containing photoactivable carbene precursors ' , European Journal of Biochemistry , vol. 132 , no. 2 , pp. 441-449 .
dc.identifier.otherPURE: 1520958
dc.identifier.otherPURE UUID: 86688de0-23b0-4770-ad4d-b5e64bd1be92
dc.identifier.otherWOS: A1983QP33500030
dc.identifier.otherScopus: 0021093289
dc.description.abstractThe lipid binding site of the phosphatidylcholine transfer protein from bovine liver has been investigated by use of phosphatidylcholine analogs which carry a diazirinophenoxy group linked to the ω-carbon of either the sn-2-[1-14C]hexanoyl (PCI) or sn-2-[1-14C]undecanoyl chain (PC II). Photolysis of the PCI(PCII)-transfer protein complex resulted in a covalent coupling of 30–40% of the label to the protein as shown by sodium dodecyl sulfate/polyacrylamide gel electrophoresis. Upon mild alkaline treatment of the photolysed complex the protein containing covalently coupled 14C-label was separated fro the noncoupled 14C-label by gel permeation chromatography. The 14C-labeled protein was degraded with protease from Staphylococcus aureus, trypsin and cyanogen bromide and specific 14C-labeled peptides were sequenced by automated Edman degradation. Major sites of coupling shown by release of radioactivity were identified as Tyr54 and the peptide segment Val171-Phe-Met-Tyr-Tyr-Phe-Asp177. Both PC I and PC II coupled extensively to Tyr54 (90% and 5% of total labeling, respectively). The remainder of the radioactivity was released from the peptide Val171-Asp177 with a distinct difference in in the pattern of release depending on whether PC I or PC II were used. Thus, coupling occurred preferentially to Tyr175 and Asp177 with PC I while Val171 and Met173 were labeled preferentially with PC II. This shift in coupling is compatible with an increasae of 0.6 nm for the sn-2-fatty-acyk cgaubs if OC I and II, assuming that the peptide Val171-Asp177 has adopted the strongly predicted β-strand configuration. These data have beeninterpreted in terms of the localization of phosphatidylcholine in the phosphatidylcholine transfer proteinen
dc.relation.ispartofEuropean Journal of Biochemistry
dc.titleIdentification of the lipid-binding site of phosphatidylcholine-transfer protein with phosphatidylcholine analogs containing photoactivable carbene precursorsen
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
rioxxterms.typeJournal Article/Review

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