Zoon K C, Smith M E
Horiz Biochem Biophys. 1982;6:123-35.
Significant advances have been made in the last four years on the purification of interferons. Components of several human and mouse interferons have been purified to homogeneity. Partial characterization of these molecules has been achieved (i.e. amino acid composition, analytical maps of radiolabelled tryptic peptides, and amino terminal amino acid sequence). In addition, preliminary evidence has been accumulated which implies that the carbohydrate portion of the molecules may play a significant role in species specificity of interferons. At present, with minute quantities of homogenous interferons available, limited structural information has been obtained. Using current production and purification schemes, sufficient material can be obtained for further amino acid sequence studies and examination of the carbohydrate portion of the molecules. Additional structural characterization of the interferon gene(s). Furthermore, as sequence homologies have been observed between human and mouse interferons, all new structural information will help to establish the interrelationships in the family of interferon proteins.
在过去四年里，干扰素的纯化工作取得了重大进展。几种人源和鼠源干扰素的成分已被纯化至同质状态。这些分子的部分特性已得到鉴定（即氨基酸组成、放射性标记胰蛋白酶肽的分析图谱以及氨基末端氨基酸序列）。此外，已积累了初步证据，表明这些分子的碳水化合物部分可能在干扰素的物种特异性中发挥重要作用。目前，由于可获得微量的同质干扰素，已获得的结构信息有限。利用当前的生产和纯化方案，可以获得足够的材料用于进一步的氨基酸序列研究以及对分子碳水化合物部分的检测。对干扰素基因进行更多的结构表征。此外，由于已观察到人和鼠干扰素之间存在序列同源性，所有新的结构信息将有助于确立干扰素蛋白家族中的相互关系。
