You obtained the following raw data when setting up a Bradford standard curve: BSA (mg/ml) 0 1 2 3 4 5 6 7 8 9 10 Absorbancy 595nm 0.225 0.310 0.420 0.510 0.610 0.720 0.810 0.915 0.950 0.980 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 0.578 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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Please make sure answers is giver 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: 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 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).
- A mixture containing only KCl and NaBr is analyzed by the Mohr Method. A 0.3172-g sample is dissolved in 50 mL water and titrated to the Ag2CrO4 endpoint, requiring 36.85 mL of 0.1120 M AgNO3. A blank titration requires 0.71 mL of titrant to reach the same endpoint. Report the % (w/w) KCl and NaBr in the sample. [Ans . 84.41 % (w /w); 17.59 % (w /w)]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.Using 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.
- 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).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 sampleCalculate the volume of BSA stock that will be required to make the standard solutions needed to create the BSA standard curve. Be sure to show your work and include the volume of 0.02 M phosphate buffer required to reach a final volume of 1 mL. From a 2,000 μg/mL BSA stock, create 1 mL of each of the following stock solutions in 0.02 M phosphate buffer using individual microcentrifuge tubes: 50 μg/mL, 250 μg/mL, 500 μg/mL, 1,000 μg/mL, 1,250 μg/mL, 1,500 μg/mL. Be sure to properly label all the microcentrifuge tubes before creating the standards.
- Viscosity measurements were done on native form of Protein XYZ and on 4 denaturants. The crude Protein XYZ was diluted to produce 5% w/v. Using the Ostwald viscometer, the following data were obtained: time, sec time, sec time, sec time, sec Denaturant Blank (Native) Native Blank (Denaturant) Denatured pH= 2.00 70 95 70 101 Temp (90 °C) 70 98 70 150 0.1M Urea 72 97 88 110 DTT 71 96 90 170 a. Calculate and tabulate the reduced viscosities (in mL/g) of the native and denatured Protein XYZ. b. Determine two most effective denaturants. c. What can be inferred with the two most effective denaturants? Dont reject if you dont know the answer!A technician at a clinical laboratory received a blood serum sample for cholesterol analysis. In order to check the reliability of the procedure, the technician repeated the assay five times and obtained the results below. Use a spreadsheet statistical analysis to estimate the mean, standard deviation and standard error of the mean (SEM) for the data. Total cholesterol in blood serum sample in mg/100 mL (mg%): 157, 154, 155, 152, 155. 2.The calibration curve shown below was used to analyze an unknown protein solution. What is the concentration of the unknown solution, if the absorbance of the unknown is 0.505? Answer in ug/mL. 1.2 y%3D0.005x+0.061 R=0.992 0.8 0.6 0.4 0.2 50 100 150 200 250 Concentration ug/ml Absorbance