Protein Quantitation

Discussion of all aspects of biological molecules, biochemical processes and laboratory procedures in the field.

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Protein Quantitation

Post by jigsaw » Sat Jul 03, 2010 5:25 am

After following the steps for either the Biuret method and the Lowry method, I am able to obtain the standard curves from the known sample absorbances. But when I match the absorbance of the unknown sample against the standard curve, I got wrong concentration of the unknown. :(

Some questions:

-Assuming the standard curve is correct; am I right to compare the absorbance of the unknown and match against the standard curve then obtaining the concentration from the x-axis?
-Is the concentration I obtain from the a-axis of the standard curve just the amount the unknown protein of the particular dilution or is it the actual concentration of the unknown. If it is just the amount of protein of a particular dilution, how do I calculate the unknown's concentration from it?

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Inland Taipan
Inland Taipan
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Post by JackBean » Sat Jul 03, 2010 8:39 am

yes, you read it from the x axis and t is of course the dilution you have used for measurement ;)

Cis or trans? That's what matters.

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