Rubinstein M, Rubinstein S, Familletti P C, Miller R S, Waldman A A, Pestka S
Proc Natl Acad Sci U S A. 1979 Feb;76(2):640-4. doi: 10.1073/pnas.76.2.640.
A method of fractionating proteins by high-performance liquid partition chromatography has been developed and used for isolation and purification to homogeneity of one of the species of human leukocyte interferon. The homogeneous interferon exhibited a sharp peak on high-performance liquid chromatography and a single narrow band on sodium dodecyl sulfate/polyacrylamide gel electrophoresis in the presence of 2-mercaptoethanol. Extraction of the gel gave a single sharp peak of antiviral activity coinciding with the protein band. The specific activity of pure interferon was found to be 2--4 X 10(8) units/mg, based on amino acid analysis. The molecular weight is 17,500--18,000.
已开发出一种通过高效液相分配色谱法分离蛋白质的方法，并将其用于分离和纯化人白细胞干扰素的一种亚型，直至达到均一性。这种均一的干扰素在高效液相色谱上呈现出一个尖锐的峰，在含有2-巯基乙醇的十二烷基硫酸钠/聚丙烯酰胺凝胶电泳上呈现出一条单一的窄带。从凝胶中提取得到的抗病毒活性呈现出一个单一的尖锐峰，与蛋白质条带一致。基于氨基酸分析，发现纯干扰素的比活性为2-4×10⁸单位/毫克。分子量为17,500-18,000。
