Page 1 Experiment 6 1· The statement below that is true of affinity purification

Question

Page 1 Experiment 6 1· The statement below that is true of affinity purification is: A) The protein of interest binds by weak forces B) The resin contains a ligand complementary to the protein binding site C) The resin contains a functionality that binds to the protein of interest D) All of the above E) Both B and C are possible. 2. In affinity chromatography, the bound protein is best eluted from the resin by A) Change pH. B) Change ionic strength. C) Add free ligand to the elution buffer D) Change temperature E) None of the above used. 3. The best measure of enzyme purity is: A) Total protein B) Total activity C) Maximum specific activity D) Fold purification E) None of the above. When BCA standards are plotted as Abs per ug protein, the standard curve has the a BCA standard curve of y 0.632 Abs/ug+0.189 Abs. If a protein solution diluted 1/10 has an absorbance of 1.287 (using 10 ul in standard BCA assayl, what is the concentration of protein in the original sample? 4. (show your work for credit). 5. How does conconavalin A-sepharose interact with HRP? How is HRP eluted? Total-TTotal TSpecific Trold iprotllactivity g mL(umol/min/mL)l protein-Activity-Activity Purification Volume Sample Pre-column 1 5 Post-column 2.5 2300 450 arm up. Tum on the computer ond

Explanation / Answer

1. C

Affinity chromatography is a purification technique whereby the protein of interest is purified by virtue of its specific binding properties to an immobilized ligand.

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