Abstract
Chymotrypsin and trypsin, when irradiated as dilute aqueous solutions under nitrous oxide both displayed anomalously low values of ${\rm D}_{37}$ . Destruction of tryptophan residues during the irradiations were, as in previous work, correlated with losses of enzymic activities by both the proteases. Interactions between the gas and the enzymes apparently affected the conformations of the proteins and, consequently, facilitated attack by radicals on the susceptible centers. Concentrated solutions of chymotrypsin irradiated under nitrous oxide did not behave anomalously when compared with previously reported data.
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