CARBOHYDRATE-BINDING PROPERTIES OF C-REACTIVE PROTEIN
The interaction of C-reactive protein (CRP) from ischemic heart disease, sepsis and cancer patients with some plasma glycoproteins was studied. Found that glycosylated forms of CRP interact differently with fibronectin, laminin, fetuin, asialofetuin and immunoglobulin G, demonstrating carbohydrate specificity for terminal galactose residues and mucin-type carbohydrate chains. This binding was inhibited by mono- and disaccharides, confirming the functional role of CRP as a lectin. Thus, it appears that structural changes in CRP molecule during various pathological processes play an important role in its carbohydrate-binding properties and are essential for its activity in vivo.