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SummaryMouse interferon, when induced by the synthetic ribopolymer, rIn.rCn, has a mol. wt. of about 150000. On brief exposure to low pH (3·5) conditions, the protein is dissociated into a smaller molecule (average mass of 38000 daltons); during this transition, the recoverable antiviral activity increases twofold. Our data support the idea that the high mol. wt. form may be a discreet interferon aggregate brought about by association of sub-units, although we cannot exclude the possibility that the antiviral protein (interferon) is simply adventitiously bound to a serum protein which antagonizes the antiviral action of interferon. This report provides additional support to the hypothesis, developed from studies with virus-induced mouse and human interferons, that apparently different interferon molecules may simply be different oligomeric species of a basic interferon subunit, α.

Interferon: the Dissociation of rIn.rCn-induced Proteins by Protonation