Mark D F, Lu S D, Creasey A A, Yamamoto R, Lin L S
Proc Natl Acad Sci U S A. 1984 Sep;81(18):5662-6. doi: 10.1073/pnas.81.18.5662.
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.
人成纤维细胞干扰素含有三个半胱氨酸残基，位于氨基酸位置17、31和141处。我们使用合成寡核苷酸引物进行定点诱变技术，将半胱氨酸-17的密码子替换为丝氨酸的密码子。由此产生的干扰素，即IFN-β Ser-17，保留了天然成纤维细胞干扰素的抗病毒、自然杀伤细胞激活和抗增殖活性。纯化的IFN-β Ser-17蛋白具有2×10⁸单位/毫克的抗病毒比活性，与纯化的天然成纤维细胞干扰素相似。此外，纯化后的蛋白在-70℃下长期储存稳定。
