학술논문
Purification to Homogeneity and Partial Characterization of Interleukin 2 from a Human T-Cell Leukemia
Document Type
research-article
Author
Source
Proceedings of the National Academy of Sciences of the United States of America, 1984 Feb 01. 81(3), 871-875.
Subject
Language
English
ISSN
00278424
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.