Interaction of Soluble and Surface-Bound Heparin Binding Growth-AssociatedMolecule with Heparin
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Authors
Fath, M.
VanderNoot, V.
Kilpeläinen, I.
Kinnunen, T.
Rauvala, H.
Linhardt, Robert J.
Issue Date
1999
Type
Article
Language
ENG
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
Alternative Title
Abstract
The interaction of heparin with heparin binding growth-associated molecule (HB-GAM) was studied using isothermal titration calorimetry (ITC) and surface plasmon resonance (SPR). ITC studies showed that, in solution, heparin bound HB-GAM with a deltaH of -30 kcal/mole corresponding to a dissociation constant (Kd) of 460 nM. The stoichiometry of interaction was 3 moles of HB-GAM per mole of heparin, corresponding to a minimum heparin binding site for HB-GAM of 12-16 saccharide residues. Kinetic measurements of heparin interaction with HB-GAM made by SPR afforded a Kd of 4 nM, suggesting considerably tighter binding when HB-GAM was immobilized on a surface. Affinity chromatography of a sized mixture of heparin oligosaccharides, having a degree of polymerization (dp) of > 14 saccharide units, on HB-GAM-Sepharose demonstrated that oligosaccharides having more than 18 saccharide residues showed the tightest interaction.
Description
FEBS Letters, 454, 105-108
Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
Full Citation
Interaction of Soluble and Surface-Bound Heparin Binding Growth-AssociatedMolecule with Heparin M. Fath, V. VanderNoot, I. Kilpeläinen, T.Kinnunen, H. Rauvala, R.J. Linhardt, FEBS Letters, 454, 105-108, 1999.