Some activity (1 to 10%) was recovered from partially purified leukocyte interferon which had been reduced by mercaptoethanol and allowed to oxidize in air. The recovery was complete if the reduced interferon was unfolded by guanidine hydrochloride or urea. Oxidation in the continued presence of these denaturants lead to incomplete recovery (3%). Carboxymethylation of reduced interferon permanently destroyed all activity. Sodium dodecyl sulphate did not cause any loss of interferon activity but did hinder successful re-oxidation in the presence of urea. The prime importance of at least one disulphide bond in interferon structure is indicated. Further confirmation was obtained by oxidative cleavage of disulphide bonds. The lack of effect of -chloro-mercuribenzoate suggests that free thiol groups are not important for antiviral action.


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