The following question is for Cellular and Molecular Biology lab.
Bradford assay was discovered by Marion M. Bradford in 1976 . It is a procedure to measure the concentration of protein in a solution .
Principle for Bradford assay is the binding of the Coomassie
Blue G250 dye to proteins . At pH 0 , both the sulfate are
negatively charged and all three nitrogens are positively charged
giving to dye +1 [ the red form of the dye ] . Around pH 1.5 , the
neutral green form of the dye predominates . At neutral pH , the
dye has a net charge of +1 [ the blue form of the dye ] . the red ,
green and bllue forms of the dye absorbs visible radiation with
absorption maxima of 470 , 650 , 550 nm , respectively . It is the
anionic form of the dye that binds to the protein . Binding of the
blue form of Coomassie Blue G250 with protein causes red shift in
its absorption spectrum ; the absorption shift maximum shift from
590 to 620 mm . Its clear to record the absorption at 620 mm . But
the absorption is recorded at 595 mm to avoid any contribution of
the green form . The dye binds more readily to the cationic residue
, lysine and arginine . this clearly indicates that the response of
the assay will depend on amino acid composition of protein , major
drawback of this assay . Modification has been made to overcome
this drawback .
COOMASSIE BLUE G250 dye we use in
Bradford assay .
We use 595 nm wavelength to get readings for Bradford assay .
The following question is for Cellular and Molecular Biology lab. What is bradford assay. Which dye...
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