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Degradation of keratan sulfate by ß‐N‐acetylhexosaminidases in GM 2 ‐gangliosidosis
Author(s) -
Yutaka Tohru,
Okada Shintaro,
Kato Tomochika,
Yabuuhi Hyakuji
Publication year - 1982
Publication title -
clinical genetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.543
H-Index - 102
eISSN - 1399-0004
pISSN - 0009-9163
DOI - 10.1111/j.1399-0004.1982.tb00963.x
Subject(s) - keratan sulfate , degradation (telecommunications) , gangliosidosis , chemistry , biochemistry , glycosaminoglycan , chondroitin sulfate , enzyme , computer science , telecommunications
We have prepared a new substrate from a keratan sulfate‐derived‐oligosaccharide (2‐acetamido‐2‐deoxyglucosyl(1–3)‐[1‐ 3 H] Galactitol), which is necessary to measure β‐N‐acetylhexosaminidase activity. This substrate was prepared from a cornea keratan sulfate by digestion with endo‐β‐galactosidase, followed by isolation of disaccharide on gel filtration chromatography and chemical desulfation. Using this substrate, we found that a striking deficiency of β‐N‐acetylhexosaminidase activity was present in the skin fibroblasts of patients with Sandhoff disease but not in Tay‐Sachs disease. Both β‐N‐acetyl‐hexosaminidase A & B contributed to the catabolism of keratan sulfate.