Magnetization-transfer techniques, such as saturation or inversion transfer, are extremely useful methods for measuring chemical-exchange rate constants which are comparable to spin-lattice relaxation rate constants of the exchanging spins. Although such determinations are relatively simple for a two-site exchange case, complications arise when multisite exchanges are involved. This severely restricts the applicability of this type of measurement, especially in whole cells and tissues where many reactants are utilized by more than one enzyme. In this paper, it is shown that a multisite exchange problem can first be reduced effectively to a two-site exchange, and a single rate constant can subsequently be measured simply and unequivocally. Application of this procedure to equilibrium and nonequilibrium chemical-exchange problems are discussed.