An enzyme is analyzed by ion exchange chromatography. The sample also contains two proteins (X and Y) in the mixture. The molecular weights (MW) of all proteins are also shown in units of kilodaltons (kDa). The proteins do not have quaternary structure. A. What type of ion exchange chromatography (anion or cation exchange), and what buffer pH, would allow scientists to maximize the binding of enzyme to the column (stationary phase) while allowing most of the other proteins to flow through? You need to indicate a specific value or narrow range of pH values. Saying "greater than or less than " x " is not sufficient. B. Explain why the conditions that you chose allow for maximal binding of enzyme to the stationary phase relative to the other two proteins. Make specific reference to how buffer pH influences the binding of this enzyme and the other two proteins to the column, and explain how a knowledge of the pI helps to determine the appropriate solvent pH