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PMID: 6608103 Published · ppublish English Journal Article

Purification to homogeneity and partial characterization of interleukin 2 from a human T-cell leukemia.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 81 ·No. 3 ·1984-02-00 ·Pages 871-5

Stern AS, Pan YC, Urdal DL, Mochizuki DY, DeChiara S, Blacher R, Wideman J, Gillis S

Abstract

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.

MeSH Terms
Amino Acid Sequence Biological Assay Chromatography, High Pressure Liquid Cloning, Molecular Cyanogen Bromide DNA Humans Interleukin-2/genetics,isolation & purification Leukemia/immunology Peptide Fragments/analysis T-Lymphocytes/analysis,immunology
Chemicals
Interleukin-2 Peptide Fragments DNA Cyanogen Bromide
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Stern A S
Pan Y C
Urdal D L
Mochizuki D Y
DeChiara S
Blacher R
Wideman J
Gillis S
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.81.3.871
Published
1984-02-00
Pages
871-5
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC344940
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.81.3.871 PMC Full Text View journal details
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