Liljeblad M, Lundblad A, Ohlson S, Påhlsson P
Department of Clinical Chemistry, University Hospital, Linköping, Sweden.
J Mol Recognit. 1998 Winter;11(1-6):191-3. doi: 10.1002/(SICI)1099-1352(199812)11:1/6<191::AID-JMR421>3.0.CO;2-4.
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) 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), 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.
