Abstract
Summary
The kinetics of inactivation at 56° and at pH 2 were different for the high-and low-molecular weight components of virus-induced and endotoxin-induced rabbit interferons. The two types of virus-induced interferons were not affected by benzoylchloride or potassium cyanate, suggesting that amino or sulfhydryl groups are not essential for their interferon activity. The integrity of disulfide bonds also seems unnecessary as indicated by the lack of effect of 2-mercaptoethanol and 100 mM thioglycolate, although 1000 mM of the latter compound partially inactivated the interferons. The effect of cyanogen bromide indicated a requirement for the γ-sulfmethyl group of methionine. Sodium metaperiodate in low concentrations rapidly inactivated purified rabbit interferons as well as crude and purified chick interferon. Although the action of periodate may suggest an essential carbohydrate moiety in the interferon molecule, this action may be equally due to an effect on protein.
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