You wish to purify an ATP-binding enzyme from a crude extract that contains several contaminating proteins. To purify the enzyme rapidly and to the highest purity, you must consider some sophisticated strategies, among them affinity chromatography. Explain how affinity chromatography can be applied to the separation, and explain the physical basis of the separation

With affinity chromatography, the specific enzyme can easily be purified. The crude extract should be in the mobile phase of the chromatography, and in the static phase, which is a solid matrix in a column, should be the ligand for the ATP binding enzyme.

As the mobile phase runs through the column containing the static phase, the ATP-binding enzyme will bind to the ligand while the other proteins will not or will bond very loosely. After this process finishes, a buffer solution washes all the weakly attached molecules present in the stationary phase. As a result, we have a matrix with the ATP-binding enzyme and ligand. To have only the enzyme, the scientist has to wash the matrix with a buffer that dissociates the enzyme-ligand union, and we obtain the enzyme in the buffer solution.

Explanation:

Affinity chromatography is a method that scientists use to separate specific molecules in a solution with different components. To separate them, it uses a particular molecule that binds to the other molecule. The strong interactions between these two elements are what make the separation from other components possible. It does not use charges or sizes like other methods, only the specific molecule.

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