What type of ion exchange resin and what buffer pH would you use to purify pepsin from an extract of pig cells? (Assume that pepsin should bind to the column resin). Anion exchanger at pH less than 3 O Cation exchanger at pH greater than 6 Cation exchanger at pH 6 Anion exchanger at pH greater than 3
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- A mixture containing glutamic acid, arginine, phenylalanine and valine was subjected to anion exchange chromatography at pH 7.0. Which of the amino acids interacted with the resin (anion exchanger) and last to be eluted with a buffer of decreasing pH? A. Glu B. Val C. Phe D. ArgWhich of the following amino acids will bind to anion exchange resin at pH 7.0?In ion-exchange chromatography, amino acids are separated on the basis of electro-static interactions and hydrophobic interactions with the resin. The chemical structure of the resin pol-ymer with a negatively charged sulfonic acid group is shown to the right. An elution profile for the aminoacids using this resin is given below. Based on the elution profile above, explain the following:
- A certain plant storage protein, after being isolated, was digested using both 8N H2SO4 and conc. Ba(OH)2. The resulting hydrolysates were then analyzed for amino acid composition using paper chromatography with EtOH-NH3-H2O (80:10:10) as the solvent system and ninhydrin as the visualizing agent. Name the amino acids found in the acid hydrolysate labelled 1-5.An 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?What volume of 0.1M NaOH (reagent) needs to be added to increase your 7.5 pH (buffer) by 0.5 pH units. The goal is to further purify MOPs (see image). Protonated form = 6.6 x 10.3^-3 mol/L Deprotonated form = 1.32 x 10^-2 mol/L Show calculations.
- It is possible to make a buffer that functions well near pH7 using citric acid, which contains only carboxylate groups. Explain.A mixture of three proteins was subjected to ion exchange chromatography using CM-cellulsoe as the stationary phase. The elution buffer had a pH of 7.5. Proteins were eluted by increasing the ionic strength of the buffer. Predict the order of elution of the following proteins:Pepsinogen, pI = 1Cytochrome c, pI = 10.6Myoglobin, pI = 6.8What is the [CH3COO−]/[CH3COOH] ratio inan acetate buffer at pH 4.00?
- The pl of alkaline phosphatase is 4.5; the pl of the DEAE cellulose is 10.5. We used a buffer of pH 7.4 to run a DEAE-cellulose as anion exchange column? Explain how did this work?An amino acid mixture consisting of lysine,leucine, and glutamic acid is to be separated by ion-exchangechromatography, using a cation-exchange resin at pH 3.5, with theeluting buffer at the same pH. Which of these amino acids will beeluted from the column first? Will any other treatment be neededto elute one of these amino acids from the column?Calculate the concentration of Y4-ion in 0.0100 M EDTA solution at pH 6. α4 = 2.2 x 10-5 for pH 6.