Anhydrous hydrogen fluoride deglycosylates glycoproteins

Abstract

Exposure of glycoproteins to anhydrous hydrogen fluoride cleaves all the linkages of neutral and acidic sugars within 1 hr at 0°C while leaving peptide bonds and glycopeptide linkages of amino sugars intact. More severe treatment with anhydrous hydrogen fluoride (3 hr at 23°C) cleaves the O-glycosidic linkages of amino sugars, but peptide bonds and the N-glycosidic linkage between asparagine and N-acetylglucosamine still remain intact. Anhydrous hydrogen fluoride, therefore, may be used for the deglycosylation of glycoproteins, thereby assisting in the further purification, proteolysis, and sequencing of the protein component. During the cleavage of glycosidic linkages by anhydrous hydrogen fluoride there is little or no degradation of the sugars themselves, thus allowing their quantitative recovery. Therefore, anhydrous hydrogen fluoride may also be useful in the analysis of complex polysaccharides.