X- and γ-irradiation of 5× 10-6 M solutions of chymotrypsin in HCl of pH 3 affects the lability of readily exchangeable hydrogen atoms in the molecule. Amino acid analyses have shown that tyrosine and tryptophan are the residues first attacked during irradiation. As tyrosine apparently has no significant role in the catalytic activity of the enzyme, conformational changes and the destruction of tryptophan residues are the routes by which radiation-induced inactivation of dilute solutions of chymotrypsin occurs.

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