Five L of a 10-to-1 dilution of a sample were added to 5mL of Bradford reagent.
ID: 3540 • Letter: F
Question
Five L of a 10-to-1 dilution of a sample were added to 5mL of Bradford reagent. The absorbance at 595 nm was 0.78 and,according to a standard curve, corresponds to 0.015 mg of proteinon the x axis. What is the protein concentration of the originalsolution? Ok so I know that the dilution means there was 10 to 1 ratioof final to intial volume of solution. And I'm guessing we aren'tsupposed to use the Beer Lambert Law since the protein is unknownso the molar absorptivity is unknown. I really don't know what todo here... Five L of a 10-to-1 dilution of a sample were added to 5mL of Bradford reagent. The absorbance at 595 nm was 0.78 and,according to a standard curve, corresponds to 0.015 mg of proteinon the x axis. What is the protein concentration of the originalsolution? Ok so I know that the dilution means there was 10 to 1 ratioof final to intial volume of solution. And I'm guessing we aren'tsupposed to use the Beer Lambert Law since the protein is unknownso the molar absorptivity is unknown. I really don't know what todo here...Explanation / Answer
Solution) Yes, you are on right track. there's a simple logic of dilution. so if we can find the dilution factor, then we can simply multiply it to the deduced concentration to find the original concentration of protein.
We have a dilution of 10-to-1, it means 1/10th dilution. and we are using only the 5?L of this dilution added in the 5ml. so, the second time we diluted it to 1000-to-1 (5?L in 5ml or 5?L in 5000?L). so, the total dilution will be 10 x 1000 = 10000.
therefore, we have to multiply it by the factor of 10000 = 0.015mg x 10000 = 150mg
Hence, the protein concentration of the original solution is 150mg/ml.
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