Interactions between the immobilized weak-affinity monoclonal IgG antibody 39.5, which is specific for the glucose-a1,4-glucose motif, and various oligosaccharides were studied with surface plasmon resonance technology. The antibody was immobilized at high levels on the surface of the sensor chip an
Detection of low-molecular-weight heparin oligosaccharides (Fragmin™) using surface plasmon resonance
✍ Scribed by Mathias Liljeblad; Arne Lundblad; Sten Ohlson; Peter Påhlsson
- Publisher
- John Wiley and Sons
- Year
- 1998
- Tongue
- English
- Weight
- 49 KB
- Volume
- 11
- Category
- Article
- ISSN
- 0952-3499
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✦ Synopsis
During the last decades there has been a growing realization of the central biological role that oligosaccharides and oligosaccharide-protein interactions play. One of the most striking examples is the use of heparin and low-molecular-weight heparin oligosaccharides (Fragmin 2 ) to modify blood coagulation. Several monoclonal antibodies directed against glycosaminoglycan structures have been produced. However, their clinical use is limited by the difficulty of detection systems for oligosaccharides. In the present study we used a monoclonal antibody directed against heparin oligosaccharides prepared by partial nitrous acid deamination of heparin. Using a biosensor (BIAcore 2 ), purified antibody was immobilized on sensor surfaces and binding of oligosaccharide was measured by surface plasmon resonance. Using this technique, it was possible to quantitate low-molecular-weight heparin oligosaccharides in nanomolar concentrations.
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