You obtained the following raw data when setting up a Bradford standard curve: BSA (mg/ml) Absorbancy 595nm 0 0.225 1 0.310 2 0.420 3 0.510 4 0.610 5 0.720 6 0.810 7 0.915 8 0.950 9 0.980
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You obtained the following raw data when setting up a Bradford standard curve:
BSA (mg/ml) | Absorbancy 595nm |
0 | 0.225 |
1 | 0.310 |
2 | 0.420 |
3 | 0.510 |
4 | 0.610 |
5 | 0.720 |
6 | 0.810 |
7 | 0.915 |
8 | 0.950 |
9 | 0.980 |
10 | 0.990 |
After blanking against a bradford-dH2O sample, the protein concentration of an unknown sample was determined using the same method and an absorbancy of 0.570 was obtained.
Set up a standard curve, excluding outliers (experimental and statistical) and determine the protein concentration in the unknown sample in mg / ml (up to 3 significant figures).
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- You obtained the following raw data when setting up a Bradford standard curve: Absorbancy BSA (mg/ml) 595nm 0.225 1 0.310 2 0.420 0.510 4 0.610 0.720 6 0.810 0.915 8 0.950 0.980 10 0.990 After blanking against a bradford-dH20 sample, the protein concentration of an unknown sample was determined using the same method and an absorbancy of 0.594 was obtained. Set up a standard curve, excluding outliers (experimental and statistical) and determine the protein concentration in the unknown sample in mg / ml (up to 3 significant figures).You obtained the following raw data when setting up a Biuret standard curve: Absorbancy BSA (mg/ml) 540nm 0 0.158 1 0.210 2 0.260 3 0.305 4 0.360 5 0.410 6 0.455 7 0.510 8 0.530 9 10 0.550 0.554 After blanking against a biuret-dH20 sample, the protein concentration of an unknown sample was determined using the same method and an absorbancy of 0.284 was obtained. Set up a standard curve, excluding outliers (experimental and statistical) and determine the protein concentration in the unknown sample in mg/ml (up to 3 significant figures).You obtained the following raw data when setting up a Biuret standard curve: BSA (mg/ml) Absorbancy 540nm 0 0.158 1 0.210 2 0.260 3 0.305 4 0.360 5 0.410 6 0.455 7 0.510 8 0.530 9 0.550 10 0.554 After blanking against a biuret-dH2O sample, the protein concentration of an unknown sample was determined using the same method and an absorbancy of 0.262 was obtained. Set up a standard curve, excluding outliers (experimental and statistical) and determine the protein concentration in the unknown sample in mg / ml (up to 3 significant figures).
- You record the absorbance of your unknown BSA sample at 0.276. What is the concentration in ug/mL of the unknown assuming you have a standard curve with the line of best fit with y=0.0001x+0.0038 as its equationUsing the data from the standard curve done previously, you record the absorbance of your extracted milk protein sample at 0.499 at 540nm. What is the mass of the protein in mg assuming you collected 10mL worth of the protein? Your standard curve should have a line of best fit with the equation y=0.0001x+0.0038.You will be given 1 mL of a 2.0 mg/mL solution of bovine serum albumin (BSA) and 1 mL of a 2.0 mg/mL solution of bovine gamma globulin (BGG). From these solutions, you will need to make 100 μL of each of the following standards using 1x MBP purification buffer as the diluent for preparation of a standard curve: 1000 μg/mL, 750 μg/mL, 500 μg/mL, 250 μg/mL, 125 μg/mL, and 0 μg/mL.
- This graph represents a standard curve from a BCA assay for protein concentration. If your BCA reaction with your unknown protein has an absorbance of 0.2, approximately what concentration of protein is in your unknown sample? Absorbance (562nm) 0.5 0.45 3 0.35 0.3. 0.25 0.15. 0.1- 0.05 ~0.1 μg/ml ~4.5 μg/ul less that 0.005 | 0.2 μg/μ. [Protein (BSA)) (pg/ml)You obtained the following raw data when setting up a Biuret standard curve: Absorbancy BSA (mg/ml) 540nm 0.158 1 0.210 0.260 0.305 0.360 0.410 0.455 7 0.510 0.530 0.550 10 0.554 What would the quality of the line-fit (R2 value) be if you do not exclude experimental outliers? (Give you answer to 4 decimal places) O-2N 34 56 o9You obtained the following raw data when setting up a Bradford standard curve: BSA (mg/ml) Absorbancy 595nm 0 0.225 1 0.310 2 0.420 3 0.510 4 0.610 5 0.720 6 0.810 7 0.915 8 0.950 9 0.980 10 0.990 Set up a standard curve. What would the quality of the line-fit (R2 value) be if you do not exclude experimental outliers? (Give you answer to 4 decimal places) Answer Skip Exit
- A gel filtration column was calibrated by measuring elution volumes for two proteins of known mass: glutamate dehydrogenase, 290 kDa with elution volume 20.8 mL; serum albumin, 37 kDa with elution volume 42.5 mL Use these values to determine the equation of the straight line graph that relates log molar mass to elution volume. The elution volume of an unknown protein was 32.2 mL. Use the equation just determined above to estimate the molar mass of the protein in kDa units. Don't round your answer until the end to ensure your answer is within the accepted range. Round your answer to the nearest whole number (e.g. If you calculated 27.52, input your answer as 28).You dissolve a 3.435 gram sample of potato in acid to determine the levels of solanine (the reason why green potatoes are poisonous) and diluted it to a total volume of 500.0 mL. You have also created a standard curve as outlined below. Solve for the ug/gram concentration of solanine in the potato sample. ppm Solanine Std. Abs 0.213 5 0.315 10 0.423 15 0.532 Unknown sample 0.314 Your Answer:a) What are the methods used for cholesterol determination? Explain the basis of the method you used in your experiment by writing.b) In the experiment conducted for the determination of cholesterol, the function of the calibration curve obtained using standard cholesterol solutions of 25-400mg/dl was determined as y= 0.0009x.Since the absorbance of the serum sample was determined as 0.28, how many mg/L is the amount of cholesterol in the sample