Abstract
Heparin is a linear polysaccharide of the glycosaminoglycan (GAG) family of carbohydrates. Heparin and other structurally related GAGs are characterized by the presence of carboxylate and sulfate groups on their polysaccharide chains giving rise to an overall negative charge. GAGs are known to mediate a host of many biological mechanisms such as cell differentiation, proliferation, metastasis and inflammation. The mechanisms of these interactions are still poorly understood hence the continued interest in their study. Due to the structural complexity and variability of functional groups in the disaccharide units that make up GAGs, their interactions with proteins continue to be a major and challenging topic in analytical, biochemical and biological studies. We present an affinity capillary electrophoresis (ACE) method to determine and compare the binding constants of heparin-derived disaccharides to histidine.
Type
Publication
J Res Anal