[38] Sulfatide-binding proteins

Add time:08/19/2019    Source:sciencedirect.com

Publisher SummaryCell surface glycoconjugates have been extensively studied as potential receptors for cell–cell and cell–ligand interactions. Carbohydrates occur on cell surface glycoproteins, glycolipids, and proteoglycans. As glycolipids containing a single oligosaccharide are readily purified and terminal structures on glycolipids are often identical to those found on glycoproteins, glycolipids are useful for examining the specificity of proteins which may bind to cell surface carbohydrates. A second class of acidic glycolipids contains sulfate esters. These lipids are found in many tissues and occur with various carbohydrate sequences. Most contain sulfate esters of galactose, but sulfation also occurs on N-acetylgalactosamine, N-acetylglucosamine, glucose, and sialic acid. Several methods have been used to study sulfatide-binding proteins. Enzymatic activation and changes in fluorescence polarization of factor XII and kininogen occur in the presence of sulfatide micelles. Numerous methods for the preparation of lipid extracts from tissues are effective for sulfated glycolipids. This chapter presents a generalized approach for characterizing sulfatide-binding proteins using immobilized sulfatides and outlines the criteria for defining the specificity of these interactions.

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