Klein M L, Bartley T D, Lai P H, Lu H S
Amgen Inc., Thousand Oaks, CA 91320.
J Chromatogr. 1988 Nov 11;454:205-15. doi: 10.1016/s0021-9673(00)88614-8.
Recombinant consensus interferon-alpha is derived from genetically modified Escherichia coli containing a synthetic gene constructed from a consensus of interferon sequences. The purified and biologically active protein has been subjected to detailed structural characterization including sequence determination and peptide isolation and identification. The homogeneous consensus interferon-alpha preparation contains two chromatographically indistinguishable homologous polypeptides with one containing an extra methionyl residue at the amino terminus. The delineated amino acid sequence of the protein is identical to that expected from the coding sequence of the gene. Correct oxidation of the molecule has been confirmed with two intramolecular disulfide linkages observed at Cys(1)-Cys(99) and Cys(29)-Cys(139).
重组复合干扰素-α 源自经过基因改造的大肠杆菌，该大肠杆菌含有一个由干扰素序列的共有序列构建而成的合成基因。纯化后的具有生物活性的蛋白质已进行了详细的结构表征，包括序列测定以及肽段的分离与鉴定。均一的复合干扰素-α 制剂包含两种在色谱上无法区分的同源多肽，其中一种在氨基末端含有一个额外的甲硫氨酰残基。该蛋白质经描绘的氨基酸序列与基因编码序列预期的序列相同。已通过在半胱氨酸（1）-半胱氨酸（99）和半胱氨酸（29）-半胱氨酸（139）处观察到的两个分子内二硫键确认了分子的正确氧化。
