Affinity chromatography is a method for separating biochemical mixtures based on specific interactions like antigen-antibody binding. It works by allowing the desired molecule to bind selectively to the stationary phase within a column. First, non-binding materials are washed away with buffer while bound molecules are later released from the stationary phase using an elution solvent. Common applications include purifying proteins, isolating enzymes, and studying drug-protein interactions. Key components are the matrix to which a ligand can bind, buffers for washing and elution, and sometimes spacer arms to improve binding of the target molecule to the ligand.