| Literature DB >> 6090949 |
T Nikaido, A Shimizu, N Ishida, H Sabe, K Teshigawara, M Maeda, T Uchiyama, J Yodoi, T Honjo.
Abstract
The human interleukin-2 (IL-2) receptor was purified by affinity chromatography using the anti-Tac monoclonal antibody, and its N-terminal amino acid sequence was determined. Complementary DNA clones were isolated and sequenced to reveal the primary structure of the IL-2 receptor precursor, which has 272 amino acid residues. The receptor is separated into two domains by a putative 19-residue transmembrane region. Two mRNAs (1.4 and 3.5 kilobases) hybridizing to the cDNA clone were found in human T cells bearing the IL-2 receptor. The cDNA directed synthesis of the IL-2 receptor in COS cells.Entities:
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Year: 1984 PMID: 6090949 DOI: 10.1038/311631a0
Source DB: PubMed Journal: Nature ISSN: 0028-0836 Impact factor: 49.962