Affinity chromatography

Affinity Chromatography is a method of separating biochemical mixtures, based on a highly specific interaction such as that between antigen and antibody, enzyme and substrate, or receptor and ligand.

Overview[edit | edit source]

Affinity chromatography is a type of chromatography that uses a biologically related agent to selectively bind to and isolate specific substances from a solution. This method can be used to purify and concentrate a substance from a solution, reduce the amount of a substance in a solution, or distinguish between different biological molecules.

Principle[edit | edit source]

The principle of affinity chromatography is based on the interaction between certain proteins and specific substances. The protein of interest will have a high affinity for a particular substance (the ligand), and this interaction is used to separate the protein from the other components of a mixture.

Procedure[edit | edit source]

The procedure of affinity chromatography involves several steps. First, a column is packed with material coated with the ligand. The mixture containing the protein of interest is then passed through the column, and the protein binds to the ligand. The column is then washed to remove unbound material. Finally, the protein of interest is eluted from the column by changing the conditions to those in which the protein-ligand interaction is not favourable.

Applications[edit | edit source]

Affinity chromatography has a wide range of applications in the fields of biochemistry, molecular biology, and medicine. It is used for protein purification, drug discovery, and diagnostics, among other things.