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- Using ultrafiltration, you concentrate a solution of Protein X as follows: Initial volume protein X = 300 mL Initial concentration protein X = 12 mg/mL Final volume protein X = 15 mL What's the final concentration of protein X in mg/mL?A mixture of proteins contains Pepsinogen (35 kDa), Fumarase (49 kDa), Transferrin (80 kDa) and Thyroglobulin (340 kDa). Rank these proteins based on the order of their elution from a gel filtration column (1 being the first one to elute and 4 as the last one). Throglobulin Pepsinogen Fumarase TransferrinIn order to separate negatively charged proteins from a mixture of neutral, positively charged and negatively proteins, you should pass the mixture of these beads through Gel filtration column, using anion exchanger beads Ion exchange chromatography column, using cation exchanger beads Gel filtration column, using cation exchanger beads Ion exchange chromatography column, using anion exchanger beads
- Which of the following options shows the correct order of fastest to slowest motion of chloride ions, glycine and proteins through the separating gel? Chloride ions > Proteins > Glycine Glycine > Chloride ions > Proteins Chloride ions > Glycine > Protein Protein > Chloride ions > GlycineA pharmacist prepares 80 mL of an isotonic solution of 1.1 %w/v Lidocaine HCl (E-value 0.2). To prepare the solution, he dissolves Lidocaine HCl in purified water to make an isotonic solution. Then he dilutes the Lidocaine HCl solution with 0.9%w/v sterile sodium chloride to complete the formulation. How many milliliters of purified water is needed to make the formulation by this method?When combining 1ml of lysosome solution with a concentration of 5mg/ml and 1ml of water what is the final concentration of the lysosome solution after adding 8.0 of a biuret reagent to the solution 2.5mg/ml 1mg/ml 0.5mg/ml 5 mg/ml
- 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).What is the order of elution of proteins on a gel-filtration column? Why is this so? What are two ways that a compound can be eluted from an affinity column? What could be the advantages or disadvantages of each?how many ml of sterile water injection must be mixed with two 4 ml vials of sterile hypertonic NaCl 7% USP to make the mixture isotonic? phar
- 4 mL of 10% TCA solution was added to 1 mL of serum and after mixing, it was waited for two minutes and filtered through non-phosphorus filter paper. 1 mL of the filtrate was taken and 13 mL of distilled water, 4 mL of sulfomolybdic acid and 2 mL of dilute SnCl2 solution were added and mixed, and after waiting for 15 minutes, the absorbances of the obtained solutions against pure water at 520 nm were read. If the function of the calibration graph obtained with 0.5-2.5 mg/mL standard phosphorus solutions is y= 0.245x + 0.107 and the absorbance value of the serum sample is 0.109, what is the amount of phosphorus in the sample?Five dialysis bags, impermeable to sucrose, were filled with various concentrations of sucrose and then placed in separate beakers containing an initial concentration of 0.6 M sucrose solution. At 10 minute intervals, the bags were weighed and the percent change in mass of each bag was graphed. Which line represents the bag that contained a solution isotonic to the 0.6 M solution at the beginning of the experiment? Which line represents the bag with the highest initial concentration of sucrose? Which line or lines represent bags that contain a solution that is still hypertonic at the end of 60 minutes? What is the best explanation for the shape of line e. after 50 minutes?There are two proteins in a pH 7 buffer, what you know is: one has a lot of Asp and Glu, the other one has a lot of Lys, Arg and His. Below which approach will get the two proteins separated? gel filtration chromatography ultracentrifugation salting out ion exchange chromatography affinity chromatography