Range: Table - link Min
||Iizuka R, Yamagishi-Shirasaki M, Funatsu T. Kinetic study of de novo chromophore maturation of fluorescent proteins. Anal Biochem. 2011 Jul 15 414(2):173-8. doi: 10.1016/j.ab.2011.03.036. p.176 table 1PubMed ID21459075
||(P.175 right column top paragraph:) "The maturation kinetics was slow
enough to monitor in real time with a spectrofluorometer and fitted
well to a single exponential curve, suggesting that the oxidation
step is the rate-limiting step in the overall chromophore
maturation process (Figs. 1 and 2 see also supplementary material).
The observed rate constant was defined as the rate constant
of de novo chromophore maturation."
||"During earlier years, the maturation rate of GFP was determined
as the rate of fluorescence development after admission of air to
anaerobically expressed GFP [ref 5]. Currently, conventional methods
to study the maturation kinetics are based on triggering protein
folding of urea-solubilized inclusion bodies [ref 9] and reoxidation of
the chromophore after chemical reduction of the mature chromophore
[refs 9–13]. However, inconsistent data have been reported (Table