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http://hdl.handle.net/1942/3267
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DC Field | Value | Language |
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dc.contributor.author | Bene, L. | - |
dc.contributor.author | Szollosi, J. | - |
dc.contributor.author | Balazs, M. | - |
dc.contributor.author | Matyus, L. | - |
dc.contributor.author | Gaspar, R. | - |
dc.contributor.author | AMELOOT, Marcel | - |
dc.contributor.author | DALE, Robert | - |
dc.contributor.author | Damjanovich, S. | - |
dc.date.accessioned | 2007-11-27T13:11:11Z | - |
dc.date.available | 2007-11-27T13:11:11Z | - |
dc.date.issued | 1997 | - |
dc.identifier.citation | CYTOMETRY, 27(4). p. 353-357 | - |
dc.identifier.issn | 0196-4763 | - |
dc.identifier.uri | http://hdl.handle.net/1942/3267 | - |
dc.description.abstract | The nature of charge distributions in membrane-bound macromolecular structures renders them susceptible to interaction with transmembrane potential fields. As a result, conformational changes in such species may be expected to occur when this potential is altered. We have detected reversible conformational change In the major histocompatibility complex (MHC) class I antigen in the plasma membrane of human JY cells, as monitored by flow-cytometric resonance energy transfer, upon reduction of the transmembrane potential (depolarization), This change increased the intramolecular energy-transfer efficiency between fluorescent donor- and acceptor-labelled monoclonal antibodies directed, respectively, to epitopes on the light (beta(2)-microglobulin) and the heavy chains of the MHC class I antigen. Repolarization of the depolarized samples restored the energy-transfer efficiency to the original values measured before depolarization, Depolarization caused similar relative changes in fluorescence resonance energy-transfer efficiency when Fab fragments were used for labelling MHC class I complex, suggesting that the observed phenomenon is not restricted to whole monoclonal antibodies. Cytometry 27:353-357, 1997. (C) 1997 Wiley-Liss, Inc. | - |
dc.language.iso | en | - |
dc.publisher | WILEY-LISS | - |
dc.subject.other | major histocompatibility complex (MHC) class I complex; fluorescence resonance energy transfer; membrane potential; MHC conformation | - |
dc.title | Major histocompatibility complex class I protein conformation altered by transmembrane potential changes | - |
dc.type | Journal Contribution | - |
dc.identifier.epage | 357 | - |
dc.identifier.issue | 4 | - |
dc.identifier.spage | 353 | - |
dc.identifier.volume | 27 | - |
local.format.pages | 5 | - |
dc.description.notes | DEBRECEN UNIV MED,DEPT BIOPHYS,H-4012 DEBRECEN,HUNGARY. DEBRECEN UNIV MED,DEPT HYG & EPIDEMIOL,DEBRECEN,HUNGARY. LIMBURGS UNIV CTR,DIEPENBEEK,BELGIUM. CONSEJO SUPER INVEST SUPER,INST QUIM FIS ROCASOLANO,DEPT BIOFIS,MADRID,SPAIN. | - |
local.type.refereed | Refereed | - |
local.type.specified | Article | - |
dc.bibliographicCitation.oldjcat | A1 | - |
dc.identifier.doi | 10.1002/(SICI)1097-0320(19970401)27:4<353::AID-CYTO6>3.0.CO;2-D | - |
dc.identifier.isi | A1997WQ83400006 | - |
item.contributor | Bene, L. | - |
item.contributor | Szollosi, J. | - |
item.contributor | Balazs, M. | - |
item.contributor | Matyus, L. | - |
item.contributor | Gaspar, R. | - |
item.contributor | AMELOOT, Marcel | - |
item.contributor | DALE, Robert | - |
item.contributor | Damjanovich, S. | - |
item.accessRights | Closed Access | - |
item.fulltext | No Fulltext | - |
item.fullcitation | Bene, L.; Szollosi, J.; Balazs, M.; Matyus, L.; Gaspar, R.; AMELOOT, Marcel; DALE, Robert & Damjanovich, S. (1997) Major histocompatibility complex class I protein conformation altered by transmembrane potential changes. In: CYTOMETRY, 27(4). p. 353-357. | - |
Appears in Collections: | Research publications |
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