Robb R J, Kutny R M, Panico M, Morris H R, Chowdhry V
Proc Natl Acad Sci U S A. 1984 Oct;81(20):6486-90. doi: 10.1073/pnas.81.20.6486.
Human interleukin 2 was separated into multiple molecular forms by selective immunoaffinity chromatography and chromatofocusing. For the most part, this heterogeneity was attributed to variations in glycosylation of the threonine residue in position 3 of the polypeptide chain. The various molecular forms of interleukin 2 had nearly identical specific activities in the in vitro proliferation assay, indicating that the glycosylation had no significant effect on this response. The entire primary sequence of interleukin 2, including the location of the intramolecular disulfide bridge, was determined by a combination of peptide mapping and protein sequencing. This information should aid in the determination of the active site(s) of the molecule.
通过选择性免疫亲和层析和色谱聚焦法,人白细胞介素2被分离成多种分子形式。在很大程度上,这种异质性归因于多肽链第3位苏氨酸残基糖基化的差异。白细胞介素2的各种分子形式在体外增殖试验中具有几乎相同的比活性,这表明糖基化对该反应没有显著影响。通过肽图分析和蛋白质测序相结合的方法,确定了白细胞介素2的完整一级序列,包括分子内二硫键的位置。这些信息应有助于确定该分子的活性位点。