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. 1984 Sep;81(18):5662-6.
doi: 10.1073/pnas.81.18.5662.

Site-specific mutagenesis of the human fibroblast interferon gene

D F Mark, S D Lu, A A Creasey, R Yamamoto, L S Lin

Site-specific mutagenesis of the human fibroblast interferon gene

D F Mark et al. Proc Natl Acad Sci U S A. 1984 Sep.

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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