Expt3 Bradford Assay- Sample Journal Article Report F09

The bradford method not only is rapid but also has

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Unformatted text preview: to 20 μg. The Bradford method not only is rapid, but also has very little interference by non-protein components. The only known interfering substances are detergents, Triton X-100 and sodium dodecyl sulfate.5, 6 Some other advantages of using the Bradford method include exhibition of a stable color which varies with proteins, high sensitivity of about 1μg, and the fact that the reagents are commercially available. Some disadvantages include the fact that the dye is destructive to protein samples, causes discoloration of protein samples, and shows significant variation with different proteins.7 This experiment seeks to obtain a standard curve for standard solutions of bovine albumin and to determine the concentration of a solution of bovine serum albumin of unknown concentration using the Bradford assay. The standard curve can be obtained by first making serial dilutions of the bovine albumin, and then adding Bradford reagent to the samples. After allowing color development to complete and the blanking of the spectrophotometer, the absorbencies of the samples can be taken. By plotting a graph of the absorbance vs. concentration, a standard curve of bovine albumin can then be obtained. In order to find the concentration of the unknown sample, the sample must first be diluted so that the absorbencies fall in the range of .01 - 0.1 μg/mL. Next, after the absorbance of the diluted unknown is found, the concentration of the diluted sample can be found by finding the point on the standard curve that matches the absorbance of the diluted sample, and then determining the corresponding concentration f...
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This note was uploaded on 03/23/2014 for the course CHEMISTRY 4141 taught by Professor Jonklaas during the Spring '13 term at Baylor.

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