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Crystalline chymotrypsin has been inactivated by ultraviolet light (2537 Å.) with a quantum yield of 0.0032 based upon loss of ability to act upon casein as a substrate. The possible significance of this datum in terms of the duo‐specificity of chymotrypsin, the integrity of the molecule as a whole and the quantum efficiency of cleavage of CONH linkages is discussed. The ultraviolet light absorption spectrum of the pure enzyme has been determined.