Cleavage of the (1→3)-2-acetamido-2-deoxy-β-d-glucopyranosyl linkage present in keratan sulfate. The A and B isoenzymes of human liver hexosaminidase (EC 3.2.1.30)

Salvatore Toma, Giovanni Coppa, Patricia V. Donnelly, Roberta Ricci, Nicola Di Ferrante, Satish K. Srivastava

Research output: Contribution to journalArticle

5 Scopus citations

Abstract

The disaccharide 2-acetamido-2-deoxy-β-d-glucopyranosyl-(1→3)-d-[1-3H]-galactitol, prepared from keratan sulfate, was rapidly hydrolyzed by the A and B isoenzymes of normal human liver hexosaminidase (EC 3.2.1.30), and by the B isoenzyme prepared from the liver of a patient who had died of Tay-Sachs disease. The disaccharide substrate was also hydrolyzed by extracts of normal, cultured-skin fibroblasts, and fibroblasts of patients with Tay-Sachs disease, whereas it was not hydrolyzed by fibroblast extracts of patients with Sandhoff disease. Thus, defective degradation of keratan sulfate, secondary to a defect of the β subunits present in the A and B isoenzymes of hexosaminidase, may contribute to the appearance of skeletal lesions in patients affected by Sandhoff disease.

Original languageEnglish (US)
Pages (from-to)271-279
Number of pages9
JournalCarbohydrate Research
Volume96
Issue number2
DOIs
StatePublished - Oct 16 1981

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Organic Chemistry

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