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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
1997-9-2
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pubmed:abstractText |
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-labeled 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 labeling MHC class I complex, suggesting that the observed phenomenon is not restricted to whole monoclonal antibodies.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0196-4763
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
27
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
353-7
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:9098627-Antibodies, Monoclonal,
pubmed-meshheading:9098627-Antigen Presentation,
pubmed-meshheading:9098627-B-Lymphocytes,
pubmed-meshheading:9098627-Cell Membrane,
pubmed-meshheading:9098627-Energy Transfer,
pubmed-meshheading:9098627-Enzyme Activation,
pubmed-meshheading:9098627-Flow Cytometry,
pubmed-meshheading:9098627-Fluorescein-5-isothiocyanate,
pubmed-meshheading:9098627-Fluorescent Dyes,
pubmed-meshheading:9098627-Histocompatibility Antigens Class I,
pubmed-meshheading:9098627-Humans,
pubmed-meshheading:9098627-Membrane Potentials,
pubmed-meshheading:9098627-Patch-Clamp Techniques,
pubmed-meshheading:9098627-Protein Conformation,
pubmed-meshheading:9098627-Rhodamines,
pubmed-meshheading:9098627-Sodium-Potassium-Exchanging ATPase,
pubmed-meshheading:9098627-Surface Properties,
pubmed-meshheading:9098627-beta 2-Microglobulin
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pubmed:year |
1997
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pubmed:articleTitle |
Major histocompatibility complex class I protein conformation altered by transmembrane potential changes.
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pubmed:affiliation |
Department of Biophysics, Medical University School, Debrecen, Hungary.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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