Purification to homogeneity and partial characterization of interleukin 2 from a human T-cell leukemia.
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.
D000595:Amino Acid Sequence; D001681:Biological Assay; D002851:Chromatography, High Pressure Liquid; D003001:Cloning, Molecular; D003488:Cyanogen Bromide; D004247:DNA; D006801:Humans; D007376:Interleukin-2 / Q000235:genetics / Q000302:isolation & purification*; D007938:Leukemia / Q000276:immunology*; D010446:Peptide Fragments / Q000032:analysis; D013601:T-Lymphocytes / Q000032:analysis / Q000276:immunology*
D007376:Interleukin-2; D010446:Peptide Fragments; D004247:DNA; D003488:Cyanogen Bromide