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
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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
- phosphate
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- 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 TransferrinAn amino acid mixture consisting of lysine, leucine, and glutamic acid is to be separated by ion-exchange chromatography, using a cationexchange resin at pH 3.5, with the eluting buffer at the same pH. Which of these amino acids will be eluted from the column first? Will any other treatment be needed to elute one of these amino acids from the column?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 have a sample at 50 ng/ul and you would like to load 400ng of this sample on a lane of an agarose gel. You also have TE buffer as diluent and 6x loading dye. Your total sample should be 12ul. Calculate the amounts of each reagent necessary to prepare this sample for gel loading.A 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?Which of the following is the densest TAG? O trimyristin O triolein tristearin tripaltristearin mitin
- you are ready to elute your MBP-BAP protein from the column using 1.5mL of TBS + 10mM maltose. Create a buffer from the provided 1x TBS and 500mM maltose stock solution.Prepare the following LB media with antibiotic added. A 100ml of LB media with 25 micro/ml of Amp and 100micro/ml of Kan final concentration. A 100ml of LB is provided and amp of Kan stock at 100 mg/ml and 50 mg/ml are also provided. Find how much each antibiotic stock solution is needed to add 100ml of LB to reach desired antibiotic concentration.Complete the table below by adding (+) or (-) if eahc sample (amino acid or protein) below will test positive or negative, respectively. sample BIURET NINHYDRIN XANTHOPROTEIC MILLON-NASSE SAKAGUCHI LEAD ACETATE PAULY HOSKIN-COLE G W H Y C R HAIR GELATIN CASEIN PEPTONE Identify the amino acid that will give the following data: BIURET NINHYDRIN XANTHOPROTEIC MILLON-NASSE SAKAGUCHI LEAD ACETATE PAULY HOPSKIN-COLE - + + + - - + - Name of amino acid: structurte of the amino acid:
- 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.N-(2-hydroxyethyl)piperazine-N'-(2-ethanesulfonic A purified protein is in a Hepes acid) buffer at pH 7 with 375 mM NaCl. A dialysis membrane tube holds a 2.0 mL sample of the protein solution. The sample tube floats in a beaker containing 1.00 L of the same Hepes buffer, but with 0 mM NaCl, for dialysis. Small molecules and ions (such as Na+, Cl-, and Hepes) can to diffuse across the dialysis membrane, but the protein cannot. Assume there are no sample volume changes during the dialysis. Calculate the final concentration of NaCl in the protein sample once the dialysis has come to equilibrium. Calculate the final NaCl concentration in the 2.0 mL protein sample after dialysis in 150 mL of the same Hepes buffer, with 0 mM NaCl, twice in succession. [NaCl] after a single dialysis: [NaCl] after a double dialysis: mM mMAn allosteric enzyme is purified and determination of its mass by gel-filtration chromatography yields 240 kDa. Chromatography in the presence of 6M urea yields a 30 kDa species and 90 kDa species. SDS-PAGE in the presence of Beta mercaptoethanol reveals 2 protein bands of 30 kDa. Describe the quatranary structure.