Purification and chemical characterization of the receptor for interleukin 2 from activated human T lymphocytes and from a human T-cell lymphoma cell line.
AUTOR(ES)
Urdal, D L
RESUMO
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 (i) a final specific activity close to the theoretical specific activity of 18,182 fmol of receptor per microgram of protein, (ii) a single band on polyacrylamide gel electrophoresis with an Mr of 55,000, and (iii) a unique, unambiguous NH2-terminal protein sequence. The receptor purified from phytohemagglutinin-activated T lymphocytes had an Mr of 60,000 but it had the same NH2-terminal protein sequence.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=391948Documentos Relacionados
- Acetylcholine receptor-specific suppressive T-cell factor from a retrovirally transformed T-cell line.
- Autocrine growth stimulation of a human T-cell lymphoma line by interleukin 2.
- Analysis of cDNA clones specific for human T cells and the alpha and beta chains of the T-cell receptor heterodimer from a human T-cell line.
- Purification to homogeneity and partial characterization of interleukin 2 from a human T-cell leukemia.
- Abelson virus transformation of an interleukin 2-dependent antigen-specific T-cell line.