scholarly journals Changes in fluorescence energy transfer between sulfhydryl fluorescent residues during ouabain sensitive Na+, K+-ATP hydrolysis.

1987 ◽  
Vol 44 (3) ◽  
pp. 311-321
Author(s):  
Masahiko SAKURAYA ◽  
Kazuya TANIGUCHI ◽  
Kuniaki SUZUKI ◽  
Akinobu KUDO ◽  
Shinji NAKAMURA ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Atp Hydrolysis ◽  
Fluorescence Energy Transfer ◽  
Fluorescence Energy

scholarly journals Actin filaments undergo limited subunit exchange in physiological salt conditions.

1982 ◽  
Vol 94 (2) ◽  
pp. 316-324 ◽  
Author(s):  
J D Pardee ◽  
P A Simpson ◽  
L Stryer ◽  
J A Spudich
Keyword(s):  
Skeletal Muscle ◽  
Energy Transfer ◽  
Actin Filament ◽  
Actin Filaments ◽  
Atp Hydrolysis ◽  
Fluorescence Energy Transfer ◽  
Subunit Exchange ◽  
Filament Assembly ◽  
Fluorescence Energy ◽  
Energy Acceptor

The exchange of actin filament subunits for unpolymerized actin or for subunits in other filaments has been quantitated by three experimental techniques: fluorescence energy transfer, incorporation of 35S-labeled actin monomers into unlabeled actin filaments, and exchange of [14C]ATP with filament-bound ADP. In the fluorescence energy transfer experiments, actin labeled with 5-(iodoacetamidoethyl)aminonaphthalene-1-sulfonic acid (IAENS) served as the fluorescent energy donor, and actin labeled with either fluorescein-5-isothiocyanate (FITC) or fluorescein-5-maleimide (FM) served as the energy acceptor. Fluorescent-labeled actins from Dictyostelium amoebae and rabbit skeletal muscle were very similar to their unlabeled counterparts with respect to critical actin concentration for filament assembly, assembly rate, ATP hydrolysis upon assembly, and steady-state ATPase. As evidenced by two different types of fluorescence energy transfer experiments, less than 5% of the actin filament subunits exchanged under a variety of buffer conditions at actin concentrations greater than 0.5 mg/ml. At all actin concentrations limited exchange to a plateau level occurred with a half-time of about 20 min. Nearly identical results were obtained when exchange was quantitated by incorporation of 35S-labeled Dictyostelium actin monomers into unlabeled muscle actin or Dictyostelium actin filaments. Furthermore, the proportion of filament-bound ADP which exchanged with [14C]-ATP was nearly the same as actin subunit exchange measured by fluorescence energy transfer and 35S-labeled actin incorporation. These experiments demonstrate that under approximately physiologic ionic conditions only a small percentage of subunits in highly purified skeletal muscle or Dictyostelium F-actin participate in exchange.

Red Laser-Induced Fluorescence Energy Transfer in an Immunosystem

2000 ◽  
Vol 280 (2) ◽  
pp. 272-277 ◽  
Author(s):  
Bernhard Oswald ◽  
Frank Lehmann ◽  
Lydia Simon ◽  
Ewald Terpetschnig ◽  
Otto S. Wolfbeis
Keyword(s):  
Energy Transfer ◽  
Laser Induced Fluorescence ◽  
Fluorescence Energy Transfer ◽  
Fluorescence Energy

scholarly journals Fluorescence energy transfer in quantum dot/azo dye complexes in polymer track membranes

2013 ◽  
Vol 8 (1) ◽  
pp. 452 ◽  
Author(s):  
Yulia A Gromova ◽  
Anna O Orlova ◽  
Vladimir G Maslov ◽  
Anatoly V Fedorov ◽  
Alexander V Baranov
Keyword(s):  
Energy Transfer ◽  
Quantum Dot ◽  
Azo Dye ◽  
Fluorescence Energy Transfer ◽  
Track Membranes ◽  
Fluorescence Energy
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