Purification of primate T cell growth factor to apparent homogeneity by reverse phase high pressure liquid...

T cell growth factor produced by the MLA144 gibbon ape lymphosarcoma T lymphocyte line was separated into two molecular forms of Mr 16,300 and Mr 14,300 which were purified 32,000-fold and 82,000-fold, respectively, and which in combination constitute the majority of biological activity of the starting material. The overall recovery of biological activity was 50%. This was accomplished with a series of chromatographic steps including reverse-phase high pressure liquid chromatography. The purified proteins are of comparable specific activities and each maintains the DNA synthesis of T cell growth factor-dependent human T cell lines at concentrations of less than approximately 18 pM (300 fg/ml).