Lesson Code: BPU-1110 (PREMIUM LESSON) Describes the use of various chromatographic methods in downstream protein purification including size exclusion, ion exchange, hydrophobic interaction and affinity chromatographies. The basics of a chromatography set-up are covered along with critical factors affecting protein separation such as column packing, resolution, column capacity, pressure and the gel matrix.

  • Category: Biopharma Processes and Equipment


After completing this e-Lesson, you will be able to:

  • Describe a general outline of a protein purification process for both intracellular and extracellular proteins
  • Describe where chromatography fits into downstream processing
  • Explain the role of different chromatographies in protein purification
  • Describe the difference between Size Exclusion Chromatography, Ion-Exchange Chromatography, Hydrophobic Interaction Chromatography, and Affinity Chromatography
  • Explain what is meant by preparative chromatography
  • Explain terms such as solubility, charge, molecular size, adsorption properties and binding specificity