Human interferon binds to albumin-agarose at low ionic strength (0.15 m NaCl) and is still retained on the column at high ionic strength (1.0 m NaCl). Apparently, the binding is quite selective as (a) most of the proteins resident in interferon preparations are not retained on the column at low ionic strength (0.15 m NaCl), and (b) several other interferons show only slight retention (mouse L cell interferon) or no retention (mouse and rabbit serum interferons) at low ionic strength (0.15 m NaCl). Human interferon, induced either by rIn·rCn or virus, can be displaced with the polarity-reducing agent, ethylene glycol. The varied strength of binding of several interferons to albumin-agarose may provide an insight into their relative hydrophobicity.
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Huang et al. (1974) studied this question.