The data in the table below were collected during a laboratory session assaying for the kinetics of Acid Phosphatase. Using a simple flow diagram, show how you would design the experiment and focus on the principles of the assay and the major components for the experimental design. Concentration (mM) Absorbance1 (410nm) Absorbance2 (410nm) 0 0.007 0.008 1 0.051 0.067 2 0.078 0.096 5 0.168 0.155 8 0.234 0.252 10 0.297 0.316 20 0.523 0.514 30 0.759 0.719
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5. The data in the table below were collected during a laboratory session assaying for the
kinetics of Acid Phosphatase. Using a simple flow diagram, show how you would design the
experiment and focus on the principles of the assay and the major components for the
experimental design.
Concentration (mM) Absorbance1 (410nm) Absorbance2 (410nm)
0 0.007 0.008
1 0.051 0.067
2 0.078 0.096
5 0.168 0.155
8 0.234 0.252
10 0.297 0.316
20 0.523 0.514
30 0.759 0.719
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- A 0.5 M phosphate buffer at pH 6.5 and a 10 mM substrate stock solution are available for preparing enzyme assays. Each assay must have a total volume of 3 mL and a final phosphate concentration of 100 mM is desired. Using the substrate concentration of 3.33 mM and 100 µL of the enzyme solution, calculate the volume of buffer, volume of substrate stock solution, and volume of water that should be place in a cuvette for the assay.1. Give the importance of carbohydrate fermentation test in biochemical testing and enumerate the enzymes that are involved. 2. What are the substances added in the culture media utilized by the organism producing hydrogen sulfide? Give 2 other media used for the production of hydrogen sulfide. 3. Explain the mechanism taking place in the hydrolysis of urea which leads to the formation of bluish red color. 4. Discuss why human blood plasma will not always yield reliable results.(b) Both laboratories used 10 micrograms of protein each in their kinetic assays. Protein concentrations weredetermined by the Bradford protein assay. Assay conditions employed in the two labs (pH, temperature,etc.) were also identical. What would be the most plausible cause for the discrepancy in the Vmax valuesfor the compound I? Explain.Recall that the Bradford assay measures total protein amounts in sample solution based on complexformation between a dye and proteins. Also, the assay solution used in both labs does not contain anyinhibitors.
- Calculate the Activity of an amylase enzyme which is diluted 1:100 times with phosphate buffer and incubated for 10 minutes at 37 degree Celsius. Given are the amount of maltose [mg] = 5.05 and the volume of enzyme used for the assay as 0.5ml.What is the need of adding DNS solution to the enzyme substrate solution bWhat is the problem in determining rates at low substrate concentration? c. Calculate the Activity of an amylase enzyme which is diluted 1:100 times with phosphate buffer and incubated for 10 minutes at 37 degree Celsius. Given are the amount of maltose [mg] = 5.05 and the volume of enzyme used for the assay as 0.5ml.The initial velocity data shown in the table were obtained for an enzyme. Each assay at the indicated substrate concentration was initiated by adding enzyme to a final concentration of 0.01 nM. Derive Km, Vmax, kcat, and the specificity constant. [S] (mM) Velocity (x10^7) 0.10 0.96 0.125 1.12 0.167 1.35 0.250 1.66 0.50 2.22 1.0 2.63
- pls explain Increasing the saturation of the ammonium sulfate is a prerequisite in isolating a target protein that is rich in Cys and Tyr residues. Which of the following techniques should be considered in accurately quantifying the isolated protein?I. Running the isolated protein in a dialysis or GFC set up.II. Using Biuret or BCA assay as the colorimetric quantitation method.III. Using Bradford or Lowry assay as the colorimetric quantitation method.A. I onlyB. II onlyC. I and IIID. I, II and III. Bradford Assay is most suitable to use when the extraction buffer is below the target protein’s pI. This is so because the protein would be morea. Positively charged allowing the CBB G-250 dye to bind via its sulfonate groups.b. Negatively charged allowing the CBB G-250 dye to bind via its sulfonate groups.c. Neutrally charged allowing the CBB G-250 dye to bind via its sulfonate groups.d. Zwitterionic allowing the CBB G-250 dye to bind via its sulfonate groups.You perform a Bradford assay to determine the concentration of isolated α-lactalbumin. You use 50 μL of a two-fold diluted solution of α-lactalbumin in the assay. You generate a standard curve with the following equation for the line: y = 0.163x + 0.082. The absorbance of your sample was 0.674 AU. What is the concentration of α-lactalbumin, in mg/mL, in your sample? Give your answer to three significant figures.present briefly the principle of size exclusion chromatography. give a brief description of the use of protein assays.
- Q. You have now carried out the Somogyi Nelson determination of reducing sugars and measured the absorption spectra of Tube 9. What is the optimum wavelength you should use to monitor the Somogyi Nelson Assay why? Table 1._SOMOGYI-NELSON DTERMENATION OF REDUCING SUGARS Tube 1 2 3 4 5 6 7 8 9 10 D-Glucose (160 µg/mL), mL 0 0 0.125 0.125 0.25 0.25 0.375 0.375 0.5 0.5 H2O, mL 0.5 0.5 0.375 0.375 0.25 0.25 0.125 0.125 0 0 D-Galactose (160 µg/mL), mL - - - - - - - - - - D-Arabinose (160 µg/mL), mL - - - - - - - - - - Glucose-Galactose Mixture, mL - - - - - - - - - - Absorbance (710 nm) 0.049 0.051 0.138 0.151 0.271 0.26 0.382 0.395 0.454 0.444 Absorbance - blank 0 0 0.088 0.101 0.221 0.21 0.332 0.345 0.404 0.394 Final [Reducing sugar]…1. In the preparation of the standard curve for protein analysis, 50 mnBSA (bovine serum albumin) dissolved in H2O to a final volume of 5mL was used as stock solution. What is the weight of BSA in 0.1 mL ofstock solution? In 0.2 mL? 2. The above mentioned aliquots (#9) which were diluted with enoughwater to a final volume of 1 mL were assayed colorimetrically andyielded the following absorbance readings:mL stock mL H2O Absorbance0.2 0.8 0.1000.4 0.6 0.2000.6 0.4 0.3000.8 0.2 0.4001.0 0.0 0.500 i. Tabulate mg BSA vs. absorbance readingii. Draw the curve where mg BSA is on x-axis and absorbance ony-axis (use graphing paper).iii. Calculate the slope of the curveiv. If a sample solution has an absorbance of 0.332, determinemg protein of the sample.Mention assays other than biuret and lowry assays that are used to detect the presence of proteins. Talk about the principle, the advantages, and the disadvantages.