dc.contributor.author | Westerman, J. | |
dc.contributor.author | Wirtz, K.W.A. | |
dc.contributor.author | Berkhout, Theo | |
dc.contributor.author | Vandeenen, L.L.M. | |
dc.contributor.author | Radhakrishnan, R. | |
dc.contributor.author | Khorana, H.G. | |
dc.date.accessioned | 2014-02-20T14:58:57Z | |
dc.date.available | 2014-02-20T14:58:57Z | |
dc.date.issued | 1983 | |
dc.identifier.citation | Westerman , 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 . https://doi.org/10.1111/j.1432-1033.1983.tb07382.x | |
dc.identifier.issn | 0014-2956 | |
dc.identifier.other | PURE: 1520958 | |
dc.identifier.other | PURE UUID: 86688de0-23b0-4770-ad4d-b5e64bd1be92 | |
dc.identifier.other | WOS: A1983QP33500030 | |
dc.identifier.other | Scopus: 0021093289 | |
dc.identifier.uri | http://hdl.handle.net/2299/12872 | |
dc.description.abstract | The 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 protein | en |
dc.format.extent | 9 | |
dc.language.iso | eng | |
dc.relation.ispartof | European Journal of Biochemistry | |
dc.subject | PCTP | |
dc.title | Identification of the lipid-binding site of phosphatidylcholine-transfer protein with phosphatidylcholine analogs containing photoactivable carbene precursors | 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.versionofrecord | https://doi.org/10.1111/j.1432-1033.1983.tb07382.x | |
rioxxterms.type | Journal Article/Review | |
herts.preservation.rarelyaccessed | true | |