Which of the following chromatographic techniques allows a faster elution of polar proteins? O Hydrophobic interaction Gel filtration Affinity lon exchange
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- When dissolved in water, an _________ donates H+; an ________ accepts H+. a. acid; base c. buffer; solute b. base; acid d. base; bufferA 0.10 M NaCl solution is (hypertonic/hypotonic/isotonic) to a 0.1M glucose solution.In the case of a protein suspension, which of the following statement/s is/are TRUE? I. The smaller ones are trapped in the gel beads. II. The proteins larger than the pore size elute first III. Trapped proteins can then be eluted with multiple solvent washes.
- A cationic microbacteriaI peptide is anaIysed using cation exchange chromatography where the packing materiaI has a negative (-) charge. Choose which buffer system is best used. trishydroxyIammonium ammonia trisaminomethane phosphateHow much of the enzyme proteinase k (solute) is required to make 250ml of a solution with a concentration of .01mg/ml? (Weight/volume ratio)Which of the following is the best explanation for a gel like this?A. Bromophenol blue was not added in the loading buffer.B. Glycine was not present in the buffer system.C. There was too much bisacrylamide in the gel solution.D. Gel was not overlaid after pouring the first gel solution.
- A solution contains 1.0 g of ephedrine sulfate in a volume of 100 mL. What quantity of sodium chloride must be added to make the solution isotonic? E value for the drug is 0.23.Please pick among these 4 Protein chromatography is typically column-based:— lon-exchange— Reverse-phase/Hydrophobic interaction— Gel-filtration— AffinityWhich of the following treatments would be most useful in removing integral membrane proteins from a membrane sample? change the pH add a detergent add salts add proteases
