Stern A S, Pan Y C, Urdal D L, Mochizuki D Y, DeChiara S, Blacher R, Wideman J, Gillis S
Proc Natl Acad Sci U S A. 1984 Feb;81(3):871-5. doi: 10.1073/pnas.81.3.871.
A method utilizing reversed-phase high-performance liquid chromatography has been developed for the purification to homogeneity of interleukin 2 (IL-2) isolated from a human T-cell leukemia. A final purification of 500,000-fold was obtained with a specific activity of pure IL-2 of 10(9) units/mg. The amino acid analysis of natural IL-2 is strikingly similar to the composition deduced from sequence analysis of a cDNA coding for human IL-2. Protein sequence analysis of CNBr-derived peptides yields data consistent with the sequence proposed from cloned cDNA. The availability of homogeneous IL-2 will allow accurate biological studies of its activity free from the contamination of the numerous lymphokine species that are known to be co-produced with IL-2 during the induction procedure.
已开发出一种利用反相高效液相色谱法从人T细胞白血病中分离白细胞介素2(IL-2)并将其纯化至同质的方法。最终获得了50万倍的纯化效果,纯化后的IL-2比活性为10⁹单位/毫克。天然IL-2的氨基酸分析结果与从编码人IL-2的cDNA序列分析推导的组成惊人地相似。对溴化氰衍生肽段进行蛋白质序列分析得到的数据与克隆cDNA所提出的序列一致。纯质IL-2的可得性将有助于对其活性进行准确的生物学研究,而不会受到诱导过程中已知与IL-2共同产生的众多淋巴因子种类的污染。