A protein that binds to glutathione can be purified using an affinity column where the solid phase is a cellulose matrix covalently attached to the molecule glutathione. What should be included in the elution buffer for this experiment to remove the protein from the column?

Affinity chromatography is one of important biochemical technique of chromatography which depends on the affinity of ligand for the receptor.Here the ligand is a protein mixture which act as mobile phase and the receptor is present in the wall of chromatography column act as stationary phase.When the protein mixture is applied on the top of the column the substances present within the protein that have high affinity for the receptor present in the walls of chromatography column binds to the later but rest of the protein pass away through the column.High concentration of ligand is used within an buffer solution to remove the desired protein from the column.

From this point of view it can be stated that in the given question high concentration of glutathione should be used to remove the desired protein from the column.