2,p-Toluidinylnaphthalene-6-sulfonate

POPOP p-bis[2-(5-phenyloxazoyl)]benzene. t ANS, anilino-8-naphthalene sulfonic acid. t TNS, 2-p-toluidinylnaphthalene-6-sulfonate. 

TEP TL TLC TMB TMP TMP TMPG TNS TPB TRIS TRITC TTAB UA USDA-FSIS Triethylphosphine Total luminescence Thin layer chromatography T etramethylbenzidine 2,4,6,8-Tetrathiomorpholinopyrimido [5,4-d] pyrimidine Trimethylphosphine S S -Trimethoxyphenylglyoxal Potassium 2-p-toluidinylnaphthalene-6-sulfonate Tetradecylpyridine bromide Tris (hydroxymethyl) aminomethane Tetramethylrhodamine isothiocyanate Tetradecyltrimethyl ammonium bromide Uric acid U.S. Department of Agriculture-Food Safety and Inspection Service... 

Plot the fluorescence emission spectra of ANS bound to serum albumin and of TNS (2, p-toluidinylnaphthalene-6-sulfonate) also bound to the protein. Are the two spectra identical Explain. 

Albani, J., Vos, R., Willaert, K. and Engelborghs, Y. (1995). Interaction between human a -acid glycoprotein (orosomucoid) and 2-p-toluidinylnaphthalene-6-sulfonate. Photochemistry and... 

Figure 1.12. Absorption spectrum of the fluorescent probe 2, p-toluidinylnaphthalene-6-sulfonate (TNS). The molecule possesses 4 electronic transitions at 223, 263, 317 and 366 nm.

In another study, we investigate electron transfer between flavocytochrome b2 and cytochrome c in presence of TNS. In principle, in absence of FMN or heme, electron transfer cannot occur between flavocytochrome b2 and cytochrome c. 2-p-toluidinylnaphthalene-6-sulfonate (TNS) is a fluorescent probe used to study the interaction between proteins, proteins and their ligands and to follow the global and local motions in proteins. TNS binds to the flavocytochrome b2 and to the flavodehydrogenase. 

Usually, when studying protein-protein interaction, fluorescence variation of the probe can indicate the type of the interaction. For example, one can find out whether the interaction between the two proteins is cooperative or not, etc... Two examples to illustrate this, we used 2,p-toluidinylnaphthalene-6-sulfonate (TNS) as a fluorescent probe to study the interaction between cytochrome c and cytochrome hj core and to follow the binding of cytochrome b2 core on flavodehydrogenase. The three proteins are extracted from the yeast Hansenula anomala (see chapter 1, paragraph 6Q. 

We performed our studies using three fluorescent probes, Trp residues, 2,p-toluidinylnaphthalene-6-sulfonate (TNS) and calcofluor white. Also, we studied the binding of hemin to a i-acid glycoprotein. Hemin is non-fluorescent and we found that it binds specifically to a i-acid glycoprotein. This experiment allowed us to prove that the glycoprotein contains a pocket where the different ligands bind (The results are detailed in chapter six). 

Albani, J, 1992, Motions studies of the human ai-acid glycoprotein (orosomucoid) followed by red-edge excitation spectra and polarization of 2-p-toluidinylnaphthalene-6-sulfonate (TNS) and of tryptophan residues. Biophysical Chemistry. 44, 129 - 137. Albani, J, 1993, A study of the interaction between two proteins, one containing a flavin mononucleotide. Journal of Biochemical and Biophysical Methods. 26, 105-112. 

McClure, W.O. and Edelman, G.M, 1966, Fluorescent probes for conformational states of proteins. 1. Mechanism of fluorescence of 2-p-toluidinylnaphthalene.6-sulfonate. A hydrophobie probe. Biochemistry 5, 1908-1918. 

ABSTRACT. The interaction of 2-p-toluidinylnaphthalene-6-sulfonate (TNS) with amylose and its related compounds in aqueous solution has been studied by both steady-state and transient fluorescence measurements. The fluorescence of TNS aqueous solution was enhanced by the addition of amylose, 3-limit dextrin, and amylopectin. The fluorescence decay of TNS bound to these polysaccharides were well described as a sum of two-exponential functions. This suggests that there are two different microenvironments at the binding sites. The fluorescence lifetime of major component for TNS-amylose system agreed with that of major component for TNS-y-cyclodextrin system. The mean rotational relaxation time of TNS bound to amylose is similar to that of the segmental motion of amylose chain. Based on these results, a configurational model for TNS-amylose complex has been proposed. 

Demchenko, A. P. (1982). On the nanosecond mobility in proteins edge excitation fluorescence red shift of paotein-bound 2-(p-toluidinylnaphthalene)-6-sulfonate. Biophysical Chemistry, 15(2), 101-109. 

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