| 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, 
											