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Amino acid sequence and post-translational modification of human interleukin 2.
Human interleukin 2 was separated into multiple molecular forms by selective immunoaffinity chromatography and chromatofocusing. For the most part, this heterogeneity was attributed to variations in glycosylation of the threonine residue in position 3 of the polypeptide chain. The various molecular forms of interleukin 2 had nearly identical specific activities in the in vitro proliferation assay, indicating that the glycosylation had no significant effect on this response. The entire primary sequence of interleukin 2, including the location of the intramolecular disulfide bridge, was determined by a combination of peptide mapping and protein sequencing. This information should aid in the determination of the active site(s) of the molecule.
PMID: 6333684 [PubMed - indexed for MEDLINE]
PMCID: PMC391949
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Cited by 11 PubMed Central articles
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The first alpha helix of interleukin (IL)-2 folds as a homotetramer, acts as an agonist of the IL-2 receptor beta chain, and induces lymphokine-activated killer cells.
Eckenberg R, Rose T, Moreau JL, Weil R, Gesbert F, Dubois S, Tello D, Bossus M, Gras H, Tartar A, et al.
J Exp Med. 2000 Feb 7; 191(3):529-40.
[J Exp Med. 2000]
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Prediction of O-glycosylation of mammalian proteins: specificity patterns of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase.
Hansen JE, Lund O, Engelbrecht J, Bohr H, Nielsen JO, Hansen JE.
Biochem J. 1995 Jun 15; 308 ( Pt 3):801-13.
[Biochem J. 1995]
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Modification and secretion of human interleukin 2 produced in insect cells by a baculovirus expression vector.
Smith GE, Ju G, Ericson BL, Moschera J, Lahm HW, Chizzonite R, Summers MD.
Proc Natl Acad Sci U S A. 1985 Dec; 82(24):8404-8.
[Proc Natl Acad Sci U S A. 1985]
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