title: Fluorescence energy transfer on erythrocyte membranes.
abstract: Stationary and time-dependent fluorescence were measured for a donor/ acceptor (DA) pair bound to membrane proteins of bovine erythrocyte ghosts. The donor N-(p-(2-benzoxazolyl)phenyl)-maleimide (BMI) and the acceptor fluram bind to SH- and NH2-residues, respectively. The fluorescence spectra and the time-dependent emission were consistent with radiationless fluorescence energy transfer (RET). Band3 protein is the only membrane spanning protein with accessible SH-groups for the coupling of BMI molecules, and therefore only acceptor binding sites on the same band3 protein were counted by the RET measurements performed. A density of RET-effective acceptor binding sites c = 0.072 nm-2 was calculated on the basis of the two-dimensional Förster-kinetics.
authors.affiliation: Institute of Physical Chemistry, University of Würzburg, Germany.
authors.forename: H M
authors.initials: HM
authors.lastname: Fuchs
authors.forename: M
authors.initials: M
authors.lastname: Hof
authors.forename: V
authors.initials: V
authors.lastname: Mudogo
authors.forename: R
authors.initials: R
authors.lastname: Lawaczeck
mesh_terms: D000818:Animals; D001665:Binding Sites; D002417:Cattle; D004735:Energy Transfer; D004910:Erythrocyte Membrane / Q000378:metabolism*; D005450:Fluorescamine / Q000378:metabolism; D007700:Kinetics; D008301:Maleimides / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism; D008856:Microscopy, Fluorescence; D013050:Spectrometry, Fluorescence; D013439:Sulfhydryl Reagents / Q000378:metabolism
chemical_list: D008301:Maleimides; D008565:Membrane Proteins; D013439:Sulfhydryl Reagents; C038669:N-(4-(2-benzoxazolyl)phenyl)maleimide; D005450:Fluorescamine