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Protein Purification problems


  • 1. In ion-exchange chromatography

  • Options
  • A. proteins are separated on the basis of their net charge
  • B. proteins are separated on the basis of their size
  • C. proteins are separated on the basis of their shape
  • D. either (b) or (c)
  • Discuss
  • 2. Which of the following may be added to stabilize the protein after yeast cells disruption?

  • Options
  • A. NaCl
  • B. Protease inhibitor
  • C. AMP
  • D. All of these
  • Discuss
  • 3. Affinity chromatography deals with the

  • Options
  • A. specific binding of a protein constituents for another molecule
  • B. protein - protein interaction
  • C. protein - carbohydrate interaction
  • D. none of the above
  • Discuss
  • 4. A purified protein sample contains 10 ?g of protein and has an enzyme activity of 1 m mole of ATP synthesized/sec (1 unit). What is the specific activity of the final purified sample?

  • Options
  • A. 1,000 units/mg
  • B. 10,000 units/mg.
  • C. 100,000 units/mg
  • D. 1,000,000 units/mg
  • Discuss
  • 5. During successful purification scheme, this may be expected that the

  • Options
  • A. specific activity increases
  • B. specific activity decreases
  • C. number of proteins in the sample decreases
  • D. both (a) and (c)
  • Discuss
  • 6. Proteins separation can be carried out on the basis of

  • Options
  • A. net charge
  • B. solubility in salt solutions
  • C. size or mass
  • D. all of these
  • Discuss
  • 7. Gel-filtration chromatography separates on the basis of

  • Options
  • A. size and shape using porous beads packed in a column
  • B. size using porous beads packed in a column
  • C. shape using porous beads packed in a column
  • D. none of the above
  • Discuss
  • 8. The best way to determine the location of protein in the purification scheme is to measure the

  • Options
  • A. rate of ATP synthesis
  • B. changes in the refractive index
  • C. UV absorption
  • D. mass spectroscopy of the protein
  • Discuss

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