Terminal monosaccharides of carbohydrate chains of glycosaminoglycans in normal human urine.

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  • ENDO MASAHIKO
    Department of Biochemistry, Tohoku University School of Medicine Department of Biochemistry, Hirosaki University School of Medicine
  • NAMIKI OSAMU
    Department of Biochemistry, Tohoku University School of Medicine Department of Orthopaedic Surgery, Tokyo Women's Medical College
  • YOSIZAWA ZENSAKU
    Department of Biochemistry, Tohoku University School of Medicine

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  • Terminal Monosaccharides of Carbohydrat

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To elucidate the mode of the exertion of glycosidase activities in the catabolism of the tissue glycosaminoglycans (GAG), the terminal monosaccharides of the carbohydrate chains of urinary GAG in the most prominent subfraction (40% Fr-1.25 M Fr) among the subfractions obtained in a previous paper (Endo et al. 1980a) were investigated. The results of determination of the reducing hexuronic acid and N-acetylhexosamine before and after digestion of the subfraction with β-glucuronidase and β-N-acetylhexosaminidase, together with previous data indicated that 0.36 and 0.37 mol of glucuronic acid and N-acetylgalactosamine, respectively, per mol of the subfraction were located at the non-reducing terminals of the carbohydrate chains. The remaining portion (0.27 mol per mol) of the non-reducing ends might be mostly occupied by the sulfated N-acetylgalactosamine residues. On the other hand, 0.25, 0.16 and 0.34 mol of glucuronic acid, N-acetylgalactosamine and xylose, respectively, per mol of the subfraction were indicated to be present at the reducing terminals of the carbohydrate chains. The remaining portion (0.25 mol per mol) of the reducing ends might be mostly occupied by the galactose residues and/or the N-acetylgalactosamine 4-sulfate residues. The present observations provided with evidence for the action of endo-β-glucuronidase and endo-β-N-acetylhexosaminidase on the tissue GAG, specifically on chondroitin sulfates.

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