Reducing terminals and molecular weights of glycosaminoglycans in normal human urine.

Endo, Masahiko; Namiki, Osamu; Yosizawa, Zensaku

doi:10.1620/tjem.132.11

Cited by 6 publications

(5 citation statements)

References 15 publications

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“…The reducing power determined by the Milner-Avigard method indicated that approximately 37 nmols of the hexuronic acid residues per mg of the subfraction were located at the reducing ends of the carbohydrate chains of the GAG (Table 1), since this method was shown to be specific for oxidation of hexuronic acid and the reducing power of the other constituent monosaccharides was negligible (Endo et al 1980d). On the other hand, the reducing N-acetylhexosamine determined by the Reissig method amounted to be 24 nmols per mg of the subfraction (Table 1).…”

Section: Reducing Terminalsmentioning

confidence: 99%

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

Endo

Namiki

Yosizawa

1980

Tohoku J. Exp. Med.

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Section: Reducing Terminalsmentioning

confidence: 99%

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

Endo

Namiki

Yosizawa

1980

Tohoku J. Exp. Med.

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“…Therefore, it is conceivable that detailed studies of human urinary GAGS provide important clues to the metabolism of tissue GAGS. Endo et al (1980c) and Maj ima et al (1984b) demonstrated the presence of …”

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confidence: 98%

Urinary glycosaminoglycans bearing glucuronic acid or iduronic acid residue at the reducing terminals.

Majima

Nakamura

Endo

1985

Tohoku J. Exp. Med.

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The urinary glycosaminoglycan was reduced with NaB [3H14, and was separated into three fractions according to molecular size by column chromatography on Sephadex G-200. The hexuronic acid residues at the reducing terminals of each fraction were quantified by the method of preferential quantitation of hexuronic acid at the reducing terminals. This method consisted of hydrolysis with trifluoroacetic acid and nitrous acid, lactonization, and paper chromatographic analysis. Both radioactive gulonolactone and idonolactone were detected in the fractions with a lower molecular size, but not in those with a higher molecular size. These observations demonstrated that the glucuronide and iduronide linkages at other-than-terminal sites of carbohydrate chains were cleaved by the processes of depolymerization of glycosaminoglycans in tissues. Therefore, it is highly likely that endo-f3-glucuronidase(s) and endo-a-iduronidase(s) which belong to the glycosidase of endo type such as hyaluronidase are involved in the catabolic degradation of glycosaminoglycans in tissues. reducing terminal ; urinary glycosaminoglycan ; glucuronic acid ; iduronic acid ; endo-glucuronidase Urinary glycosaminoglycans (GAGS) are metabolites of tissue proteoglycans which are catabolized by concerted actions of proteases, glycosidases and sulfatases in various tissues (Varadi et al. 1967;Constantopoulos et al. 1969; Wasteson and Wessler 1971; Endo et al. 1980a, b). Therefore, it is conceivable that detailed studies of human urinary GAGS provide important clues to the metabolism of tissue GAGS. Endo et al. (1980c) and Maj ima et al. (1984b) demonstrated the presence of

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“…Therefore, identification of the reducing terminal sugar unit of urinary ChS provides a clue to the elucidation of the mechanism of catabolism of tissue proteochondroitin sulfate. Endo et al (1980c) and Maj ima et al (1984a, b) indicated that a fraction of urinary glycosaminoglycans (GAGS) has a glucuronic acid residue at the reducing terminal by using the Milner-Avigad reaction (1967) and the isotope labeling method. Then, Endo et al (1980c) stated that xylose residue might be present at Received January 24, 1985; accepted for publication March 28, 1985.…”

mentioning

confidence: 99%

“…Endo et al (1980c) and Maj ima et al (1984a, b) indicated that a fraction of urinary glycosaminoglycans (GAGS) has a glucuronic acid residue at the reducing terminal by using the Milner-Avigad reaction (1967) and the isotope labeling method. Then, Endo et al (1980c) stated that xylose residue might be present at Received January 24, 1985; accepted for publication March 28, 1985. All sugars mentioned in this paper are of D configuration except for gulonic acid, gulonolactone, iduronic acid, idonolactone and fucose which are of z configuration.…”

mentioning

confidence: 99%

“…Endo et al (1980c) and Maj ima et al (1984a, b) indicated that a fraction of urinary glycosaminoglycans (GAGS) has a glucuronic acid residue at the reducing terminal by using the Milner-Avigad reaction (1967) and the isotope labeling method. Then, Endo et al (1980c) stated that xylose residue might be present at the reducing terminal of the urinary GAGS, on the basis of the molar ratios of xylose to serine obtained by sugar and amino acid composition analyses. However, the questions related to the identification of xylose and other sugars except for gucuronic acid have remained to be solved .…”

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Reducing terminals of urinary chondroitin sulfate.

Matsue

Takagaki

Honda

et al. 1985

Tohoku J. Exp. Med.

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Human urinary chondroitin sulfate isolated from the cetylpyridinium chloridecomplex of the non-dialyzable fraction of the pooled urine was subjected to ethanol fractionation, successive enzymic digestion with neuraminidase and mucopolysaccharidases, and anion exchange chromatography. The gas liquid chromatographic analyses of the acetyl and butaneboronic acid ester derivatives of the reduced terminal sugar units after treatment with sodium borohydride plus hydrolysis revealed that 42° of the urinary chondroitin sulfate was bound to peptide through xylose. The reducing terminal sugar units of the peptide-free form consisted of 34.6% of xylose, 22.4% of galactose, 16.4% of glucose of unknown origin and 26.6% of glucuronic acid. These observations showed that the xyloside, galactoside and glucuronide linkages at non-terminal sites of carbohydrate chains of chondroitin sulfate were cleaved in tissues. It was thus suggested that the endo-types of /3-xylosidase, $-galactosidase and $-glucuronidase, which act on proteochondroitin sulfate are present in tissues. reducing terminal ; urinary chondroitin sulfate ; galactose ; glucuronic acid ; xylose Human urinary chondroitin sulfate (ChS), depolymerized and desulfated to various extents, has been regarded as the final degradation products in the catabolism of tissue proteochondroitin sulfate (Wasteson and Wessler 1971; Endo et al. 1980 b). Therefore, identification of the reducing terminal sugar unit of urinary ChS provides a clue to the elucidation of the mechanism of catabolism of tissue proteochondroitin sulfate. Endo et al. (1980c) and Maj ima et al. (1984a, b) indicated that a fraction of urinary glycosaminoglycans (GAGS) has a glucuronic acid residue at the reducing terminal by using the Milner-Avigad reaction (1967) and the isotope labeling method. Then, Endo et al. (1980c) stated that xylose residue might be present at Received January 24, 1985; accepted for publication March 28, 1985. All sugars mentioned in this paper are of D configuration except for gulonic acid, gulonolactone, iduronic acid, idonolactone and fucose which are of z configuration.

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Reducing terminals and molecular weights of glycosaminoglycans in normal human urine.

Cited by 6 publications

References 15 publications

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

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

Urinary glycosaminoglycans bearing glucuronic acid or iduronic acid residue at the reducing terminals.

Reducing terminals of urinary chondroitin sulfate.

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