Galactosylation as a tool for the stabilization and immobilization of proteins

This paper presents a brief overview of the role that the carbohydrate moieties of biologically active glycoproteins play in the stabilization and oriented immobilization of these proteins on solid supports. The synthetic galactosylation of hydrophobic areas or their surroundings on the protein surface improves the structural stability of native proteins against inactivation by the interaction of water with hydrophobic clusters. The lowering of the degree solvation of tyrosine residues in galactosylated trypsin and the model substance N-carbobenzoxy-L-glutamyl-L-tyrosine was proved by Raman spectroscopy. D-Galactose residues can be selectively oxidized, either with periodate or enzymatically, and the aldehyde groups thus formed are used for the immobilization of glycoproteins on solid supports with hydrazide groups under mild conditions.