Homework Answers
Answer - The correct answer is 2.83 µg.
Explanation -
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0. 0 0026 0.987 What is the protein concentration in an unknown food sample with the...
In biochemistry, we use a 'Bradford Assay' to calculate the concentration of protein in a sample....
In biochemistry, we use a 'Bradford Assay' to calculate the concentration of protein in a sample. This method uses the same principles of the standard curve from this experiment. In a Bradford Assay, a standard curve is prepared using a known protein, typically Bovine Serum Albumin (BSA), but rather than measuring the density, we can measure a different property - its 'absorbance'. The graph below is representative of a standard curve from a Bradford Assay (with the line equation displayed...
please answer 1 and 2 table 4 protein concentrations 1. Determine the protein concentrations for your...
please answer 1 and 2
table
4
protein
concentrations
1. Determine the protein concentrations for your positive and negative control and your test sample (Table 4) using the protein standard curve you constructed. Include Table 4 and your protein concentrations in your response. Do these results seem accurate to you? Did they differ from what you expected for the food item you brought into class? 2. What is the R2 value of your known protein concentrations plotted against their absorbency?...
A Bradford assay was carried out to measure protein concentration. The absorbance of five standard samples...
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 ...
In lab, you diluted your unknown protein solution by combining 14 ?L of unknown protein solution...
In lab, you diluted your unknown protein solution by combining
14 ?L of unknown protein solution with enough
PBS buffer to obtain a total volume of 100 ?L, then added 1000 ?L Bradford reagent. After waiting ten
minutes, the absorbance at 595 nm was 0.206. Using the standard
curve from the previous question, calculate the total concentration
of protein (in ?gmL) in the original sample.
Slope = 0.02371 Intercept = 0.01132 r2
= 0.973
4. (a) Determine the experimental concentration of protein in the unknown solution in mg/mL using the...
4. (a) Determine the experimental concentration of protein in the unknown solution in mg/mL using the Part II Data Table and the equation on page 2 for the absorbance assay at 280 nm. Hint: Convert the molar concentration (M or moles/liter) of BSA from absorbance assay at 280 nm method to mg/mL, assume that the molecular weight of BSA = 66.5 kDa [7 points 6500 g/mol Post-lab 10 Report Form: Determination the Concentration of a Protein You must show your...
Both Biuret and Bradford methods was used to determine unknown concentrations of both BSA and BIg....
Both Biuret and Bradford methods was used to determine unknown concentrations of both BSA and BIg. The methods followed is described in detail in the Background section. The following results was obtained: Table 1: Absorbance at 595nm obtained for different concentrations of protein standards using the Bradford method [Protein] (mg/ml) 0.00 0.125 0.25 0.50 0.75 1.00 1.50 2.00 Unknown Abs. BSA 0 0.130 0.350 0.620 0.870 1.120 1.400 1.60 1.050 Abs. BIg 0 0.080 0.130 0.360 0.520 0.650 0.850 1.080...
You have 0.5 mL sample of protein extract (absorbance 0.5930) with a concentration of 181.2 ug/mL....
You have 0.5 mL sample of protein extract (absorbance 0.5930) with a concentration of 181.2 ug/mL. How many ug (micrograms) of sample do you have?
3. Suppose that an unknown sample is analyzed spectrophotometrically at the same wavelength that was used...
3. Suppose that an unknown sample is analyzed
spectrophotometrically at the same wavelength that was used for the
standard curve and the absorbance was found to be 0.196. Use the
standard curve to find the concentration of the unknown.
1. Calculate the concentration of a solution prepared by adding 15.00 mL of 1.98 x 10-3 M KMnO, from a buret into a 50.00 mL volumetric flask, which is then filled to the 50.00 mL graduation mark with distilled water. Hint:...
the molar absorptivity of the copper complex in chloroform at 436.0nm is 13,000 M-1 cm-1 which...
the molar absorptivity of the copper complex in chloroform at
436.0nm is 13,000 M-1 cm-1 which is useful
for the determination of Cu2+ concentrations as low as
10-6g/ml.
III. Interpretation of Results (a) Calibration curve Calculate the Cu2+ concentration of each standard solution in ug/mL (ug = 100 gram). Alternatively, ug/mL = ppm (part per million). Plot the net absorbance (= absorbance of standard - absorbance of blank) versus the concentration of each standard solution. sample volume 0 absorbance 0.061...
FOOD DYE SPECTROPHOTOMETRY POST LAB HELP PLEASE!!! 1) If the unknown concentration is higher than the...
FOOD DYE SPECTROPHOTOMETRY POST LAB HELP PLEASE!!! 1) If the unknown concentration is higher than the data points of your calibration curve, should you go ahead and find the absorbance to determine its concentration using the equation generated by your calibration curve? Why or why not? Explain your answer. 2)Are there any concerns if you wait an hour or two after you calibrate the spectrophotometer to obtain the absorbance of your solutions and unknown? Explain your answer. 3) Are there...
In biochemistry, we use a 'Bradford Assay' to calculate the concentration of protein in a sample. This method uses the same principles of the standard curve from this experiment. In a Bradford Assay, a standard curve is prepared using a known protein, typically Bovine Serum Albumin (BSA), but rather than measuring the density, we can measure a different property - its 'absorbance'. The graph below is representative of a standard curve from a Bradford Assay (with the line equation displayed...
please answer 1 and 2
table
4
protein
concentrations
1. Determine the protein concentrations for your positive and negative control and your test sample (Table 4) using the protein standard curve you constructed. Include Table 4 and your protein concentrations in your response. Do these results seem accurate to you? Did they differ from what you expected for the food item you brought into class? 2. What is the R2 value of your known protein concentrations plotted against their absorbency?...
In lab, you diluted your unknown protein solution by combining
14 ?L of unknown protein solution with enough
PBS buffer to obtain a total volume of 100 ?L, then added 1000 ?L Bradford reagent. After waiting ten
minutes, the absorbance at 595 nm was 0.206. Using the standard
curve from the previous question, calculate the total concentration
of protein (in ?gmL) in the original sample.
Slope = 0.02371 Intercept = 0.01132 r2
= 0.973
4. (a) Determine the experimental concentration of protein in the unknown solution in mg/mL using the Part II Data Table and the equation on page 2 for the absorbance assay at 280 nm. Hint: Convert the molar concentration (M or moles/liter) of BSA from absorbance assay at 280 nm method to mg/mL, assume that the molecular weight of BSA = 66.5 kDa [7 points 6500 g/mol Post-lab 10 Report Form: Determination the Concentration of a Protein You must show your...
3. Suppose that an unknown sample is analyzed
spectrophotometrically at the same wavelength that was used for the
standard curve and the absorbance was found to be 0.196. Use the
standard curve to find the concentration of the unknown.
1. Calculate the concentration of a solution prepared by adding 15.00 mL of 1.98 x 10-3 M KMnO, from a buret into a 50.00 mL volumetric flask, which is then filled to the 50.00 mL graduation mark with distilled water. Hint:...
the molar absorptivity of the copper complex in chloroform at
436.0nm is 13,000 M-1 cm-1 which is useful
for the determination of Cu2+ concentrations as low as
10-6g/ml.
III. Interpretation of Results (a) Calibration curve Calculate the Cu2+ concentration of each standard solution in ug/mL (ug = 100 gram). Alternatively, ug/mL = ppm (part per million). Plot the net absorbance (= absorbance of standard - absorbance of blank) versus the concentration of each standard solution. sample volume 0 absorbance 0.061...
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