8. The recommended range of sample volume to be loaded onto the gel filtration chromatography column is within 1-5 percent of the column's total volume. 9. A calculated partition coefficient (Kav) that is greater than 1 indicates that no solute or protein entered the pores of the gel filtration chromatography column resin/beads. 10. In a medium with pH 5.5, a protein with an IpH of 4.5 is expected to migrate towards the anode.
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- 2. Provide a one-sentence broad generalization regarding the % acrylamide one should use in SDS PAGE gels and the MW range targeted. 3. Name and give the purpose of each component in the electrophoresis buffer (specify type and pH) used for SDS PAGE.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.3. How many milliliters would you need to prepare a 10-2 dilution from a 10ml starting culture?
- One tenth mL of a protein solution was diluted with 2.5 mL of water. The A280 of the diluted solution was 0.25. How many mL of the original protein solution and water should be mixed to make 1.0 mL of solution of A280 = 0.80?An extraction Buffer, EB(200 mM Trish-HCL(Ph 8), 250 mM NaCl, 25 mM EDTA, 0.5% SDS) is used for DNA extraction from cells. Use their stock solutions to prepare their respective working concentrations for the given working volume of EB. Stock Solutions are: 1M Tris-HCL(pH~8) 0.5M EDTA 0.8M NaCl 10% SDS Show final calculaed values in the table given below. Component 1L EB 500 ml EB 250ml EB 100ml EB 200mM Tris-Hcl 250mM NaCl 25mM EDTA 0.5% SDS dH2O2 if there is a stock solution of 2000 (ug/ml) , is it possible to use SERIAL DILUTION to generate the following 8 tubes with their concentrations? A 2000 (ug/ml) B 1500 (ug/ml) C 1000 (ug/ml) D 750 (ug/ml) E 500 (ug/ml) F 250 (ug/ml) G 125 (ug/ml) H 0 (ug/ml)
- 1. What is the function of each step or reagent used in the isolation of casein from milk? Reagents: a. Warm distilled water b. Vinegar c. Ethanol 2. What are the three general steps involved in the isolation of proteins? Discuss or briefly describe the purpose of each step. 3. Suggest a simple procedure (or test) to verify if the final product you obtained is indeed casein.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? The mentioned aliquots (#9) which were diluted with enough water to a final volume of 1 mL were assayed colorimetrically and yielded 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.1. Which of the following statement/s is/are TRUE for the protein sample?* The sample will give a positive result to Biuret test. All of A, B and C The sample will give a positive result to Ninhydrin test. The sample will give a positive result to Xanthoproteic test. 2. Extremely high pH causes folding of the protein molecules. * The statement is CORRECT. The statement is INCORRECT. 3.Negative with Biuret Test but positive with Ninhydrin Test, Xanthoproteic Test and Millon’s Test Glycine Tryptophan Tyrosine Methionine Albumin
- 1. Why must the solution to be tested with ninhydrin be neutral? 2. Are Xanthoproteic and Millon Nasse tests satisfactory for use in the urinary examination for protein? Why? 3. Which test can be used to show up to what stage the hydrolysis of a protein proceeds? Why?I. Identify the approximate amount of the visible band II. Describe the trouble shooting problem from the gel1- Describe any errors in your technique. How could you improve upon your technique in order to get a better and more accurate standard curve graph? 2-Estimate (from your data) the [Protein] of your unknown (0.103) based on comparing to the standards. Include the correct unit. This estimate should be an integer (no decimals).