In the page, other samples are in blue colour but the acetic acid extract alone is in yellow colour? what is the reason? whether the protein bands could be visible in the well after running the gel?
This is due to the disturbance of pH of running Tris glycine electrode buffer please adjust the pH 8.3.
Bromophenol blue is a pH indicator. if the pH becomes acidic, it'll turn transparent and then yellow. acidic pH is not what you want to have when you run negatively charged proteins (SDS) through alkaline gel and buffer. thus, you should either adjust the pH or evaporate the acetic acid.
I agree with the comments from David and would like to add one more. SDS can not bind proteins at acid pH, therefore you will not get any good protein separation of this sample. You need to adjust the pH of this sample at least ~ 6.0 to make sure that SDS will bind the proteins in this sample.
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