For an assay using a standard curve, why must unknown samples and standards be assayed simultaneously?
In case of standard curve, the unknown samples and standards must be simultaneously assayed as this helps in making better comparison between the two samples. It helps in calculating the absorbance and by finding out the absorbance value, it helps in finding out the value of the unknown sample. As the unknown sample and standard values are assayed together it helps in making a comparison about the values. The standard curve is basically plotting the graph from the data values of the sample and hence it is important that one is aware of the amount present in the unknown sample. As the unknown sample and standard is assayed together simultaneously, it helps in drawing the graph and also extrapolating the data
For an assay using a standard curve, why must unknown samples and standards be assayed simultaneously?
A Bradford assay was carried out to measure protein concentration. The absorbance of five standard samples and two unknown samples are listed in the table below. The Bradford reaction mixture (1 ml) was prepared as follows: 100 μl sample A or sample B + 200 μl Bradford reagent + 700μl 0.9% NaCl solution sample ID concentration (mM) absorbance (O.D.) std 1 100 0.78 std 2 50 0.4 std 3 25 0.18 std 4 12.5 0.08 std 5 0 0 ...
3. Why can we assume in the Biuret assay that BSA (used in the standards) and casein (our protein of unknown concentration) give about the same amount of A550 per mg? 4. To calibrate the Ninhydrin assay, glycine was used. Draw the structures of Glycine, Arginine, and Threonine. Instead of glycine, would it be acceptable to use Arginine or Threonine? Explain!
you assay an unknown sample and its concentration falls below the linear range of your standard curve. what can you do to solve this problem?
1. You have generated the following standard curve after a Bradford Assay to measure Absorbance vs samples of known BSA concentrations. Now you need to determine the amount of protein in two mitochondria samples taken from fish, one taken from fish under normal conditions and the other taken from fish under oxidative stress. The absorbance reading for the normal fish fraction was A595=175, and the absorbance reading for the stressed fish fraction was A595= 275 Bradford Assay Standard Curve y...
They performed a BSA assay to determine the concentration of an unknown solution X. The graph below is the BSA standard curve. In the cuvette, you add 25 ul of the unknown solution X, 200 ul of the Bradford’s reagent and 775 ul dH2O. You obtain an absorbance of 0.58 at 595nm. Use all the information to calculate the concentration of the unknown solution X. Show work Y- 0.0457x R^2- 0.9901
4. Bradford assay. In your prac you used the Bradford assay to determine the protein concentration (1.5 marks) a) Explain at a molecular level how the color development of the assay works. Answer must be less than 100 words. (0.5 marks) b) Explain why you can use Bovine Serum Albumin as standard protein to determine the concentration of milk proteins. Answer must be less than 50 words. (0.5 marks) c) Why is it important to use diluted milk fraction samples...
using my standard curve I need to determine the concentration of glucose in the unknown the equation is y=-0.1741x+0.7254 the absorbance for the unknown is 0.201
What is the minimum number of samples that could make a standard line on the calibration curve and why do we use many samples
using my standard curve I need to determine the concentration of glucose in the unknown Volume of Glucose added (ml) Glucose Concentration (mol/l) % Transmittance Absorbance 0.00 2.7001 x 10-3 17.6 0.754 1.00 2.7001 x 10-5 31.2 0.506 2.00 5.4002 x 10-5 41.5 0.382 3.00 8.1003 x 10-5 60.9 0.215 Unknown 63.0 0.201 Using the standard determine the concentration of glucose in the unknown. The equation is y=-0.1741x+0.7254. this is all the information thats needed
Why must the standard curve pass through the origin (the zero point on both axes)?