Abstract
Human fibroblast interferon has three cysteine residues, located at amino acid positions 17, 31, and 141. Using the technique of site-specific mutagenesis with a synthetic oligonucleotide primer, we changed the codon for cysteine-17 to a codon for serine. The resulting interferon, IFN-beta Ser-17, retains the antiviral, natural killer cell activation, and antiproliferative activities of native fibroblast interferon. The purified IFN-beta Ser-17 protein has an antiviral specific activity of 2 X 10(8) units/mg, similar to that of purified native fibroblast interferon. In addition, the purified protein is stable to long-term storage at -70 degrees C.
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