Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2832808 | Molecular Immunology | 2008 | 7 Pages |
Abstract
Early work examining the interactions of IL-2 and the urinary glycoprotein uromodulin led to the suggestion that IL-2 was a lectin with specificity for high-mannose and mannan ligands. Subsequent studies have attributed various roles to these properties, some critical to the cell proliferative activity of IL-2. In an attempt to verify the reported interaction between IL-2 and mannose containing carbohydrate ligands we studied two biologically active forms of IL-2 using various techniques including affinity chromatography, equilibrium dialysis, and NMR methods. Despite previous reports we have not been able to demonstrate that IL-2 possesses the ability to bind carbohydrate.
Keywords
HSQCFCSIL-2THGP2-MEnuclear magnetic resonance2-mercaptoethanolBSAbovine serum albuminEDTAEthylenediaminetetraacetic acidInterleukin-2ELISAEnzyme-linked immunosorbent assayNMRequilibrium dissociation constanturomodulinfetal calf serumHeteronuclear Single Quantum CorrelationAffinity chromatographyTamm-Horsfall glycoprotein
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Authors
Giuseppe A. Papalia, James M. Rini,