Fluorescence lifetimes of the tryptophan residues in ornithine transcarbamoylase

Biochemistry ◽  
1993 ◽  
Vol 32 (50) ◽  
pp. 13925-13932 ◽  
Author(s):  
Wei Hai Shen
1988 ◽  
Vol 42 (8) ◽  
pp. 1405-1412 ◽  
Author(s):  
M. Baek ◽  
W. H. Nelson ◽  
P. E. Hargraves ◽  
J. F. Tanguay ◽  
S. L. Suib

The intrinsic steady-state fluorescence due to tryptophan has been obtained from monospecific cultures of fourteen plankton algae of various genera. Fluorescence decay profiles of protein tryptophan residues were obtained for eight marine plankton algae. Each organism exhibits a strong maximum in its emission spectrum at 320–340 nm when excited at 290 nm. Iodide quenching and denaturization experiments with 8 M urea provide strong evidence for the assignment of the 320–340 nm fluorescence to protein tryptophan. Most importantly, the decay of this bacterial protein tryptophan fluorescence has been described. The observation that characteristic protein-tryptophan fluorescence lifetimes have been obtained for each organism suggests that measurements of fluorescence lifetimes may be helpful in the rapid characterization of algae. Direct application will likely be found in combination with the measurement of other luminescence parameters.


2010 ◽  
Vol 1247 ◽  
Author(s):  
Rocío Calderón-Villajos ◽  
Carlos Zaldo ◽  
Concepción Cascales

AbstractControlled reaction conditions in simple, template-free hydrothermal processes yield Tm-Lu2O3 and Tm-GdVO4 nanocrystals with well-defined specific morphologies and sizes. In both oxide families, nanocrystals prepared at pH 7 reaction media exhibit photoluminescence in ∼1.95 μm similar to bulk single crystals. For the lowest Tm3+ concentration (0.2 % mol) in GdVO4 measured 3H4 and 3F4 fluorescence lifetimes τ are very near to τrad.


1988 ◽  
Vol 7 (4) ◽  
pp. 373-378 ◽  
Author(s):  
O. Gustafsson ◽  
M. Larsson ◽  
P. Sigray

1986 ◽  
Vol 261 (27) ◽  
pp. 12814-12819 ◽  
Author(s):  
E Eisenstein ◽  
L T Duong ◽  
R L Ornberg ◽  
J C Osborne ◽  
P Hensley

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