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Summary
Deoxyribonuclease I (DNase I) has been irradiated in dilute solution in aerobic and anaerobic conditions, using α- and γ-radiations with a view to investigating an earlier suggestion that radiation-induced inactivation was caused by the destruction of a tryptophan residue at the active site.
The relationship between the loss of tryptophan, and inactivation of the enzyme, both by chemical attack and by irradiation, was studied.
The action of a specific inhibitor confirms the importance of tryptophan to the enzymic activity of DNase I. DNase II did not show such a marked dependance on tryptophan for its activity, and parallel studies were made on this enzyme for comparison.
However irradiation studies indicated that there was no correlation between tryptophan destruction and the radiation-induced inactivation of DNase I. It is suggested that inactivation may result from changes in conformation.