Purification and chemical characterization of the receptor for interleukin 2 from activated human T lymphocytes and from a human T-cell lymphoma cell line.

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Abstract
The cell surface receptor for interleukin 2 plays a central role in the biology of this T-cell growth factor. A combination of affinity chromatography, high-performance liquid chromatography and NH2-terminal protein sequencing was used to purify and chemically characterize the interleukin 2 receptor both from phytohemagglutinin-activated T cells and from the human T-cell lymphoma cell line HuT-102. The receptor isolated from HuT-102 cells was purified 16,000-fold to homogeneity as evidenced by a final specific activity close to the theoretical specific activity of 18,182 fmol of receptor per .mu.g of protein, a single band on polyacrylamide gel electrophoresis with an MW of 55,000 and a unique, unambiguous NH2-terminal protein sequence. The receptor purified from phytohemagglutinin-activated T lymphocytes had MW of 60,000 but it had the same NH2-terminal protein sequence.