Final answer:
In Affinity Chromatography, proteins interact with immobilized ligands, enzyme substrates or inhibitors, and antibodies. These specific interactions allow for the purification and study of proteins through selective binding and subsequent elution under altered conditions.
Step-by-step explanation:
In Affinity Chromatography, proteins can interact with three specific types of substances depending on the target protein's properties and the purpose of the chromatography. These substances include:
- Ligands: Proteins bind to ligands that have been immobilized on a chromatographic support. This interaction is highly specific and is the basis for the separation of proteins.
- Enzyme substrates or inhibitors: For proteins that are enzymes, substrates or inhibitors can be immobilized as affinity ligands.
- Antibodies: Proteins can also bind to specific antibodies that have been immobilized on the chromatographic matrix, allowing for the purification of proteins such as antigens.
The specific interaction between the protein of interest and the immobilized substance (ligand, enzyme substrate/inhibitor, or antibody) allows for selective binding, and elution is often achieved by changing the conditions to release the bound proteins. These interactions are key to understanding how Affinity Chromatography can be used to purify and study proteins.