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Differentiation of 3-O-sulfated heparin disaccharide isomers: Identification of structural aspects of the heparin CCL2 binding motif
| Content Provider | Paperity |
|---|---|
| Author | Girardi, Matthew Leary, Julie A. Meissen, John K. Esko, Jeffrey D. Lawrence, Roger Sweeney, Matthew D. |
| Abstract | The presence of 3-O-sulfated glucosamine residues in heparin or heparan sulfate plays a role in binding to antithrombin III and HSV infection. In this study, tandem mass spectrometry was used to differentiate between two heparin disaccharide isomers containing variable sulfate at C6 in a common disaccharide and C3 in a more rare one. The dissociation patterns shown by MS2 and MS3 were clearly distinguishable between the isomers, allowing their differentiation and quantitation. Using this technique, we show that an octasaccharide with 11 sulfate groups with high affinity for inflammatory chemokine CCL2 does not contain 3-O-sulfated disaccharides. |
| Starting Page | 652 |
| Ending Page | 657 |
| File Format | HTM / HTML |
| ISSN | 10440305 |
| DOI | 10.1016/j.jasms.2008.12.002 |
| Issue Number | 4 |
| Journal | Journal of The American Society for Mass Spectrometry |
| Volume Number | 20 |
| e-ISSN | 18791123 |
| Language | English |
| Publisher | Springer US |
| Publisher Date | 2009-04-01 |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
| Subject | Spectroscopy Structural Biology |