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001-es BibID:	BIBFORM046278
Első szerző:	Matkó János (biológus)
Cím:	Luminescence quenching by long range electron transfer : a probe of protein clustering and conformation at the cell surface / Matko Janos, Jenei Attila, Wei Taiyin, Edidin Michael
Dátum:	1995
ISSN:	0196-4763
Megjegyzések:	Quenching of luminescence from fluorescent and phosphorescent probes by nitroxide spin labels with a long range electron transfer (LRET) mechanism (44,45) has been tested as a tool to monitor association/clustering and conformational changes of cell surface proteins. The membrane proteins were labeled with monoclonal antibodies or Fab fragments conjugated with luminescent probes or water-soluble nitroxide spin labels. The method was tested as a probe of 3 different aspects of protein-protein association involving class I MHC molecules: (1) interaction between the heavy and light chains of the MHC molecules, (2) clustering, self-association of MHC molecules, (3) proximity of MHC molecules to transferrin receptors of fibroblasts or surface immunoglobulin molecules of B lymphoblasts. The extent of quenching upon increasing the fractional density of the quencher was sensitive for protein association in accordance with earlier immunoprecipitation and flow cytometric Forster-type energy transfer (FCET) data obtained on the same cells. These data suggest that the LRET quenching can be used as intra- or intermolecular ruler in a 0.5-2.5 nm distance range. This approach is simpler (measurements only on donor side) and faster than many other experimental techniques in screening physical association or conformational changes of membrane proteins by means of spectrofluorimetry, flow cytometry, or microscope based imaging.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Cytometry. - 19 : 3 (1995), p. 191-200. -
További szerzők:	Jenei Attila (1966-) (biofizikus) Wei, Taiyin Edidin, Michael
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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