Abstract
A new, mild method for the splitting of N-linked oligosaccharides from glycoproteins includes treatment of glycoproteins (ovomucoid, flavoprotein, ribonuclease B, hemagglutinin, or transferrin) with 2 m LiBH 4 in 25m m LiOH-50m m Li citrate-70% aqueous tert-butyl alcohol (5 h, 45°), followed by hydrolysis of the resulting glycosylamine with aqueous acetic acid. The oligosaccharides formed were easily isolated by gel filtration and cation-exchange chromatography in 60–80% yields. The reaction was accompanied by the intense reductive cleavage of peptide bonds with formation of amino alcohols, but N-deacetylation of hexosamine was completely excluded. The optimal conditions of this reaction were chosen by use of a model glycopeptide, 2-acetamido-4- O-(2-acetamido-2-deoxy-β- d-glucopyranosyl)-1- N-(4- l-aspartoyl)-2-deoxy-β- d-glucopyranosylamine.
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