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Please use this identifier to cite or link to this item: http://hdl.handle.net/1942/3267

Title: Major histocompatibility complex class I protein conformation altered by transmembrane potential changes
Authors: Bene, L.
Szollosi, J.
Balazs, M.
Matyus, L.
Gaspar, R.
AMELOOT, Marcel
DALE, Robert
Damjanovich, S.
Issue Date: 1997
Publisher: WILEY-LISS
Citation: CYTOMETRY, 27(4). p. 353-357
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.
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.
URI: http://hdl.handle.net/1942/3267
DOI: 10.1002/(SICI)1097-0320(19970401)27:4<353::AID-CYTO6>3.0.CO;2-D
ISI #: A1997WQ83400006
ISSN: 0196-4763
Type: Journal Contribution
Appears in Collections: Research publications

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