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The M1 protein of influenza virus is a highly hydrophobic polypeptide that is resistant to enzyme cleavage during incubation in water solutions. We show here that the M1 protein that is immobilized on an insoluble activated support (thiopropyl Sepharose-6B) by means of a thiol–disulfide exchange reaction acquires sensitivity to trypsin. After tryptic digestion noncysteine-containing peptides of M1...