Fractionation and characterization of urinary heparan sulfate excreted by patients with Sanfilippo syndrome
| Autor: | Hideo Kochi, Atsushi Kimura, Koichi Tsurumi, Shiro Hayashi, Masai Koseki |
|---|---|
| Rok vydání: | 1984 |
| Předmět: |
Male
Adolescent Chemical Phenomena Mucopolysaccharidosis Oligosaccharides Fractionation General Biochemistry Genetics and Molecular Biology Mucopolysaccharidosis III chemistry.chemical_compound Sulfation medicine Humans Trisaccharide Glycosaminoglycans Sanfilippo syndrome chemistry.chemical_classification Chemistry General Medicine Heparan sulfate Mucopolysaccharidoses Oligosaccharide medicine.disease carbohydrates (lipids) Carbohydrate Sequence Biochemistry Deamination Sephadex Child Preschool Female Heparitin Sulfate |
| Zdroj: | The Tohoku Journal of Experimental Medicine. 144:227-236 |
| ISSN: | 1349-3329 0040-8727 |
| DOI: | 10.1620/tjem.144.227 |
| Popis: | KIMURA, A., HAYASHI, S., KOSEKI, M., KOCHI, H. and TSURUMI, K. Fractionation and Characterization of Urinary Heparan Sulfate Excreted by Patients with Sanfilippo Syndrome. Tohoku J. exp. Med., 1984, 144 (3), 227-236 -Urinary heparan sulfates (HS) from two siblings with mucopolysaccharidosis (MPS) III-B were fractionated by chromatography with Dowex 1 and Sephadex G-50. Their Mr ranged from 1600 to 8000, and 95% of them were included in the region less than 5000. Fractions with lower Mr contained larger amounts of O- and N-sulfates. The chemical analysis and deaminative cleavage of HS suggested that an intact HS molecule was composed of some blocks rich in GlcNAc and GlcUA and other blocks rich in GlcNS, IdUA and O-sulfate. GlcNAc-UA-GlcNS-UA-GlcNAc-UA-GlcNAc was found to be a major oligosaccharide of HS with Mr less than 1800. Trisaccharides, GlcNAc-GlcUA-aMan and GlcNAc-IdUA-aMan, were released from the nonreducing end of HS-oligosaccharides by deaminative cleavage. They carried 0-3 moles of ester sulfate. GlcNAc-IdUA-aMan was more sulfated than the other. The release of significant amounts of nonsulfated trisaccharide conform to the enzyme defect in this disease. Urinary HS obtained from another patient with MPS III were examined by the same way. Although the patient was not examined enzymatically, the structure of urinary GAG suggested a defect of α-N-acetylglucosaminidase in the patient. |
| Databáze: | OpenAIRE |
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