Matsuda S, Utsumi J, Kawano G
J Interferon Res. 1986 Oct;6(5):519-26. doi: 10.1089/jir.1986.6.519.
Recombinant mouse interferon-beta (rMuIFN-beta) produced in Escherichia coli was purified to homogeneity and characterized. The purified protein exhibited a single band of Mr 19,900 on SDS-polyacrylamide gel electrophoresis under both reducing and nonreducing conditions, and also exhibited a single band on native polyacrylamide gel electrophoresis at pH 4.3. The observed molecular weight corresponded to that of the polypeptide moiety of natural MuIFN-beta of Mr 19,700. The amino acid composition and the amino-terminal sequence of the purified rMuIFN-beta were identical to those predicted from cDNA sequence. These results indicate that the purified protein is a nonglycosylated MuIFN-beta, which forms no disulfide-linked dimer and probably exists as a monomeric form.
对在大肠杆菌中产生的重组小鼠干扰素-β（rMuIFN-β）进行了纯化并表征。纯化后的蛋白质在还原和非还原条件下的SDS-聚丙烯酰胺凝胶电泳中均呈现出一条分子量为19,900的条带，并且在pH 4.3的天然聚丙烯酰胺凝胶电泳中也呈现出一条单一的条带。观察到的分子量与天然Mr 19,700的小鼠干扰素-β的多肽部分的分子量相对应。纯化后的rMuIFN-β的氨基酸组成和氨基末端序列与从cDNA序列预测的一致。这些结果表明，纯化后的蛋白质是一种非糖基化的小鼠干扰素-β，它不形成二硫键连接的二聚体，可能以单体形式存在。
