Why does Coomassie Brilliant Blue R interact differently with different proteins? A partial answer.
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چکیده
منابع مشابه
Criticism of the use of Coomassie Brilliant Blue G-250 for the quantitative determination of proteins.
The quantitative determination of proteins in biological fluids, using Coomassie Brilliant Blue G-250, was evaluated. Compared with the biuret method, the Coomassie Blue G-250 method needs a much shorter time for analysis and has a greater sensitivity. The sensitivity of the dye for albumin is significantly greater than for globulins. The standard curves for the biuret method are more linear th...
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Expelling of dyestuff into water resource system causes major thread to the environment. Adsorption is the cost effective and potential method to remove the dyes from the effluents. Therefore, an attempt was made to study the adsorption of dyestuff (Methylene Blue (MB), Bromophenol Blue (BPB) and Coomassie Brilliant Blue (CBB)) by α-chitin nanoparticles (CNP) prepared from Penaeus monodon (Fabr...
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The binding of CBB to BSA was investigated under imitated physiological conditions employing different optical spectroscopic techniques viz., fluorescence emission, UV-vis absorption and FTIR. Fluorescence quenching data obtained at different temperatures suggested the presence of dynamic type of quenching mechanism. The values of K and n for CBB-BSA system were calculated and found to be 4.20 ...
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The binding of coomassie brilliant blue G (CBB) to bovine serum albumin (BSA) was investigated under simulative physiological conditions employing different optical spectroscopic techniques viz., fluorescence emission, UVâvisible absorption and FTIR. Fluorescence quenching data obtained at different temperatures suggested the presence of dynamic type of quenching mechanism. The binding constant...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1985
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)39198-6