| Autor: |
Berra, Bruno, Gasperi, Rita, Rapelli, Silvana, Okada, Shintaro, Li, Su-Chen, Li, Yu-Teh |
| Zdroj: |
Neurochemical Pathology; Apr1986, Vol. 4 Issue 2, p107-117, 11p |
| Abstrakt: |
The material derived from defective degradation of glycoproteins, which accumulates in brain and liver of a patient with G gangliosidosis type I, was investigated, and the structure of the main storage compounds determined. For comparison, brain and liver of a patient with G gangliosidosis type II were also analyzed. Analysis of the glycopeptides obtained after pronase digestion of the defatted residue indicates the storage of glycoprotein-like material in type I, but not in type II. Treatment with endo-β-galactosidase showed that the stored material contained N-acetyllactosamine repeating units. Two major oligosaccharides, OS I and OS II, were isolated after the enzyme treatment, whose structures are: GlcNAcβ1→3 Gal (OS I) and Galβl→4GlcNAcβ1→3 Gal (OS II). Treatment with exo-β-galactosidase transformed the trisaccharide OS II into the disaccharide OS I, indicating that the deficiency of β-galactosidase in G gangliosidosis type I, but not in type II, also affects glycoprotein catabolism, leading to the accumulation of glycopeptides containing terminal β-galactosyl residues and N-acetyllactosamine repeating units. These results indicate the severe impairment in the catabolism of glycoconjugates with β-linked galactose in type I, although this impairment is not as pronounced in type II. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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