CARBOHYDRATE-PEPTIDE LINKAGES IN GLYCOPROTEINS AND MUCOPOLYSACCHARIDES FROM BRAIN |
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Authors: | R U Margolis R K Margolis D M Atherton |
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Institution: | Department of Pharmacology, New York University School of Medicine, New York, NY 10016 and Department of Pharmacology, State University of New York, Downstate Medical Center, Brooklyn, NY 11203, U S A. |
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Abstract: | Abstract— Treatment of glycopeptides, prepared from glycoproteins of rat and rabbit brain, with NaOH-NaBH4 leads to the destruction of a portion of the serine, threonine and galactosamine present, and the appearance in acid hydrolysates of alanine, α-aminobutyric acid and galactosaminitol. These results indicate that N-acetylgalactosamine at the reducing end of oligosaccharide chains in brain glycoproteins is linked O-glycosidically to the hydroxyl groups of serine and threonine residues. 2-acetamido-1-(L-β-aspartamido)-l,2-dideoxy-β-D-glucose was also detected after partial acid hydrolysis of the alkali-stable glycopeptides, and most of the carbohydrate in brain glycoproteins appears to be linked by N-acetylglucosaminylasparagine linkages. The results of the treatment of the sulphated mucopolysaccharides from bovine brain with alkaline-borohydride indicate that the polysaccharide chains in chondroitin sulphate and heparan sulphate are linked exclusively to serine. |
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