Explain how gel filtration chromatography works. What type of gel will you used when the protein size is 2500 Da? Explain.
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Explain how gel filtration chromatography works. What type of gel will you used when the protein size is 2500 Da? Explain.
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- Explain the differences between gel electrophoresis and column chromatography. Address the principles behind each separation. Why do large molecules migrate more easily in one method and with more difficulty in the other? Which method generated the most precise results?In Gel filtration chromatography, when will you stop collecting eluents if sample is not colored?In a gel filtration chromatography, what type of gel must be used when the protein size is 2500 Da? Explain.
- Gel-filtration chromatography is a useful method for removing salts, such as ammonium sulfate, from protein solutions. Describe how such a separation is accomplished.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.In gel electrophoresis and column chromatography, why do large molecules migrate more easily in one method and with more difficulty in the other? Which method generated the most precise results?
- The SDS-PAGE protocol requires 0.5L of running buffer for the gel apparatus. The stock running buffer comes as a 20x concentrate. How should you prepare your running buffer? 50ml 20x stock + 450ml deionized water 450ml 20x stock + 50ml deionized water O 250ml 20x stock + 250ml deionized water 25ml 20x stock + 500ml deionized water 25ml 20x stock + 475ml deionized water 2ml 20x stock + 500ml deionized water O 100ml 20x stock + 400ml deionized waterYou are performing an enzyme reaction that works the same way as your wheat germ acid phosphatase (WGAP) assay. First, you dissolve 10.0 umol of product into 1.00 ml of buffer, and measure an absorbance of 0.500. Your cuvette has a 1.00 cm pathlength. Next, you perform the enzyme assay. Your enzyme solution has a concentration of 20.0 ug/ml. 1) Mix 0.250 ml substrate buffer with 0.250 ml enzyme 2) Incubate 20.0 min 3) Stop the assay with 0.500 ml NaOH 4) Read an absorbance of 0.200 *The units required for each answer in this problem are given. Answers to all three parts should be rounded to a maximum of three decimal places. Do not enter any letters. What is the extinction coefficient (ml/umol/cm) of the product? What is the catalytic activity (umol/min) measured in your assay? What is the specific activity (umol/min/ug) measured in your assay?Gel used in electrophoresis is/are: a. Agarose gel b. Polyacrylamide plain gel c. Polyacrylamide SDS impregnated Polyacrylamide gel (Sodium dodecyl sulphate)
- Discuss in chemical detail the mechanism of action (how it works) of IMAC. Compare and contrast gel filtration chromotography with IMAC. Discuss the pros and cons for each technique. Why would a scientist prefer one technique over another? In what situations would one technique be more viable than the other?You are running a size exclusion column to purify your 25 kDa protein from a lysate mixture. The void volume for the column is 10 mL, while the elution volume is 50 mL.The resin is used to separate proteins from 10 kDa up to 100 kDa.After running 75 mL of buffer through the column, you stop and run samples on an SDS-PAGE gel on fractions that showed absorbance values at 280 nm.On your SDS-PAGE gel, none of lanes shows a band at 25 kDa. What is the best possible explanation for the results? y. Your elution buffer did not have a high enough salt concentration to elute your protein. z. Your protein is not globular so runs at a different molecular weight on the SDS-PAGE gel. aa. You did not run enough buffer through the column to elute your protein. bb. Your protein does not absorb at 280 nm due to no solvent exposed aromatic groups.How is 10^4 derived? Please show all calculation steps. # of cells per mL = (Average)*DF*10^4