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1. In Gel filtration chromatography, when will you stop collecting eluents if sample is not colored?
2. How does SDS-PAGE separate proteins and peptides from each other? Explain.
3. Explain the Donnan Membrane Phenomenon. Why is it important for the homeostasis of the cell?
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- 1. In Gel filtration chromatography, when will you stop collecting eluents if sample is not colored? 2. Explain the Donnan Membrane Phenomenon. Why is it important for the homeostasis of the cell?2 a. You are trying to purify protein C from a mixture of proteins noted in the above Table. If you had only one type of column to choose from, which one would allow you to purify protein C with the least number of contaminants? Size exclusion column Ion exchange column Affinity chromatography using glucose as the bait Affinity chromatography using NAD as the bait Please explain why you chose the column above based upon the properties of the column AND the proteins in the Table.1. Why must the solution to be tested with ninhydrin be neutral? 2. Are Xanthoproteic and Millon Nasse tests satisfactory for use in the urinary examination for protein? Why? 3. Which test can be used to show up to what stage the hydrolysis of a protein proceeds? Why?
- 1. A mixture of proteins with the following properties were purified using cation exchange chromatography. Which of the following peaks correspond to the correct protein?Protein M- pI- 11, size- 60 KdaProtein N- pI- 8, size- 112 KdaProtein O- pI- 6, size- 280 KdaProtein P- pI- 4, size- 36 Kda[N.B: I was trying to upload pictures, but it was interrupting, Peak C is the highest peak, Peak D is lowest, Peak B is higher than D; however lower than C and A, Peak A is lower than C only, higher than B and D] a) Peak A is P b) Peak C in N c) Peak D is P d) Peak B is O e) Peak A is M 2. Which transition state analog is the most effective competitor for serine protease such as Chymotrypsin?a) R-C=O-NH-R’b) R-C=O(CH3)-NH-R’c) R-CH(OH)-CH(NH2)-R’d) R-CH(OH)-NH-R’e) R-CH=NR’ 3. If a 14C fatty acid labelled with C14 is fed to a cow, after 30 minutes of Beta oxidation, where will the C14 be found?a) Acetyl coA b) Propionyl coA c) Glutamine d) Glucose 4. How many carbons will…Both of the regular intravenous solutions administeredin medicine, normal saline and lactated Ringer’ssolution, are isotonic. Why is this important?1. The chromatography solvent is very polar as it contains alcohol, an acid and water. Based on this information, list all the polar amino acids and arrange them from most polar to least polar.
- We're attempting to isolate and purify a single protein. Gel filtration chromatography columns allow us to distinguish proteins based on which protein property?1. Suppose Biuret test is conducted to a solution of RNA. Will it give a positive result or not? Explain your answer. ____________________________________________________________________ ____________________________________________________________________ 2. Why is Molisch’s test used for the determination of presence of pentose in the hydrolysate? What other test could be used for this? ____________________________________________________________________ ____________________________________________________________________Consider the following properties of the protein components of a sample mixture as provided in the table below: 1. if the mixture is subjected to gel filtration chromotography which protein component elute first? 2. if the mixture is subjected to isoelectric focusing which protein will stop m oving nearest to the positive electrode? 3. if the mixture is subjected to cation-exchange chromotography using a buffer at ph 7 which protein will bind to the resin? 4.if the mixture is subjected to SDS-PAGE which protein will be at bottomost portion of gel? 5.if the mixture is subjected to hydrophobic interaction chromotography which protein will bind most strongly to the resin?
- Design an assay with purified phycocyanin to test protein stability using 500ml of 95% ethanol. Then do the same with 2 M sodium chloride. Make each step clear.In dialysis protein purification technique, the mebrane tubing needs to be pre-wet. Why? What would happen if we used a dry membrane?Using the chart below, can you produce a two-step procedure that demonstrates protein purification in protein D from the other proteins? Would you use a size and/or an ion-exchange chromatography? 1. Sketch two chromatograms that demonstrates this behavior.