Ion exchange chromatography is used to separate charged molecules from complex biological samples. The charged molecules bind to a solid support carrying an opposite charge to the molecule. Proteins contain regions of charged groups on the surface which interact with the ion exchange groups immobilised on the solid support (resin column). Immobilised proteins are eluted by changing either pH or the salt gradient or a combination of both. This lab activity involves preparation of a crude protein extract and running ion exchange chromatography for isolation of proteins.
- The principle ion exchange chromatography
- Immobilisation of protein on ionic charged columns
- Factors influencing binding and elution of proteins in ion exchange chromatography
- Hands-on ion exchange chromatography lab activity
Also required: Spectrophotometer and cuvettes or microplate reader and microplate (optional), low speed centrifuge for 1,5 to 2 ml tubes.
Informace o dodávce: Supplied with components needed for hands-on experimentation for six workstations of 4 to 5 students or 24 to 30 students. Supplied with Teacher’s Guide and separate Student’s Guides.