25 Jul WHICH OF THE FOLLOWING OPTIONS IS THE BEST WAY TO PURIFY THIS PROTEIN?
You kn Show more CHECK ALL ANSWERS THAT APPLY. THERE MAY BE MORE THAN ONE ANSWER FOR EACH QUESTION. Thank you! You know the molecular weight of the monomeric Enc protein; however you would like to get an idea of what the pI of the protein is. From the following options what is the best way to estimate that? [ ] SDS-PAGE [ ] Size-exclusion chromatography [ ] 2-D gel electrophoresis [ ] Salt out Protein analysis: You are attempting to separate a 60-subunit protein Enc from a mixture of other proteins. Each monomer has a molecular weight of 29 kDa. At pH 7.0 the protein has a net charge of -12. Which of the following options is the best way to purify this protein? [ ] Salt out via ammonium sulfate precipitation and ion exchange chromatography [ ] Ion exchange chromatography and size-exclusion chromatography [ ] SDS-PAGE and affinity chromatography [ ] Salt out via ammonium sulfate precipitation and affinity chromatography I have two purified samples of the enzyme PKA (Protein Kinase A). One sample is treated with cAMP (cyclic AMP) while the other other is not. The cAMP-treated sample shows 2 bands on a non-denaturing PAGE whereas the untreated sample shows only 1 band. What is the best explanation for this result? [ ] PKA is activated by cAMP. The active enzyme would show more bands. [ ] PAGE causes denaturation of the PKA. [ ] cAMP unfolds PKA. [ ] cAMP dissociates the regulatory and catalytic subunits of PKA. You have some protein sample and you want to quantify it using a spectrophotometer. You take a small sample of protein and put it in a quartz cuvette take a wavelength scan and observe absorbance intensity at 280 nm. Which of the following is likely to make it so that you can analyze protein using a spectrophotometer? [ ] Very concentrated protein sample [ ] Proteins are composed of chiral molecules [ ] The number of Trp and Tyr residues found in the amino acid sequence [ ] All of the above Show less
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