Determination of dissociation constants for a heparin-binding domain of amyloid precursor protein and heparins or heparan sulfate by affinity capillary electrophoresis |
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Authors: | McKeon Jocelyn Holland Lisa A |
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Institution: | Chemistry Department, West Virginia University, Morgantown, WV, USA. |
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Abstract: | Dynamic affinity capillary electrophoresis (ACE) was used for determining the binding constants between heparin-like glycosaminoglycans and the (96-110) heparin-binding domain of amyloid precursor protein (APP). The migration time shift of the (96-110) APP peptide was monitored as the concentration of heparin was increased in the background electrolyte. The compounds investigated included low-molecular-weight heparin, porcine mucosa heparin, and heparan sulfate. Change in mobility as a function of glycosaminoglycan concentration was plotted using both linear regression (Scatchard analysis) and nonlinear regression. Dissociation constants (K(d)) were determined and compared for both sets of analyses with the low-molecular-weight heparin giving the most reproducible results and best fit with a K(d) value of 3.9 microM. |
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