Abstract
The mixed disulfide of a Green-Fluorescent Protein with an Alexa 532 fluorescent label showed FRET, with quenching of the GFP emission. Reductive cleavage of this disulfide bond destroyed the FRET, giving a change in the ratios of fluorescence intensity at the wavelengths corresponding to the GFP and the Alexa dye. Cleavage by glutathione (second order rate constant at pH 7.4 was 1.18 ± 0.02 × 10 2 Min -1 min -1) was faster than for sodium cyanoborohydride. Copyright © 2005 The Chemical Society of Japan.
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CITATION STYLE
Zhang, W., Suzuki, M., Ito, Y., & Douglas, K. T. (2005). A chemically modified green-fluorescent protein that responds to cleavage of an engineered disulphide bond by Fluorescence Resonance Energy Transfer (FRET)-based changes. Chemistry Letters, 34(6), 766–767. https://doi.org/10.1246/cl.2005.766
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