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.
After taking this e-Lesson you will be able to:
- Explain the role of different chromatographic methods in protein purification.
- Describe where chromatography fits into downstream processing.
- Construct a general outline of a protein purification process for both intracellular and extracellular proteins.
- Explain what is meant by preparative chromatography.
- Describe the difference between "Size Exclusion", "Ion-Exchange", "Hydrophobic Interaction" and "Affinity" chromatography.
- Explain terms such as solubility, charge, molecular size, adsorption properties and binding specificity.
You can download a PDF product brochure here: