Fluorescence energy transfer on erythrocyte membranes.
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.
Fuchs
H M
HM
Institute of Physical Chemistry, University of Würzburg, Germany.
Hof
M
M
Mudogo
V
V
Lawaczeck
R
R
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
D008301:Maleimides; D008565:Membrane Proteins; D013439:Sulfhydryl Reagents; C038669:N-(4-(2-benzoxazolyl)phenyl)maleimide; D005450:Fluorescamine