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Method development for studying the interactions between antithrombin and heparin
Linköping University, The Department of Physics, Chemistry and Biology.
2008 (English)Independent thesis Advanced level (degree of Magister), 20 points / 30 hpStudent thesis
Abstract [en]

Antithrombin (AT) is one of the most important anticoagulant factors in the blood, and its effects are increased by the interaction with glycosaminoglycans, especially heparin. AT appears in two additional variants, other than the native form, and those variants have antiangiogenic properties and also bind to heparin. AT is found in two distinct isoforms (alfa, beta) where the difference lie in the degree of glycosylation. This project has shown interesting results regarding the dependence of calcium ions on the binding between heparin and antithrombin. The results show that the beta-isoform increases its affinity for heparin in the presence of calcium in contrast to the alfa-isoform, which shows a decrease in the heparin affinity under the same conditions. This project has also given results that after further investigation and development could be used for an improved set-up of the immobilisation of AT variants in a surface plasmon resonance system. The results show that immobilisation of a protein in the reference channel gives a better shielding effect between the negatively charged heparin molecules and the negatively charged dextran matrix. Furthermore a more significant difference was seen between the two heparin moieties used during binding affinity studies, especially for native AT.

Place, publisher, year, edition, pages
Institutionen för fysik, kemi och biologi , 2008. , 54 p.
Keyword [en]
Antithrombin, heparin, calcium, surface plasmon resonance, fluorometry
National Category
Biochemistry and Molecular Biology
URN: urn:nbn:se:liu:diva-11208ISRN: LITH-IFM-EX--07/1887--SEOAI: diva2:17618
2008-02-25, Bikupan, B-huset, Linköpings Universitet, Linköping, 13:15
Available from: 2008-03-11 Created: 2008-03-11

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