TY - JOUR
T1 - 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)
AU - Toma, Salvatore
AU - Coppa, Giovanni
AU - Donnelly, Patricia V.
AU - Ricci, Roberta
AU - Ferrante, Nicola Di
AU - Srivastava, Satish K.
N1 - Funding Information:
This work was supported by grants AM-26482-01 and NS-14966 from the National Institutes of Health, U.S. Public Health Service; by grant l-610 of the March of Dimes Birth Defects Foundation; and by grant R-7821 from the Easter Seal Research Foundation of the National Easter Seal Society for Crippled Children and Adults.
PY - 1981/10/16
Y1 - 1981/10/16
N2 - 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.
AB - 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.
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U2 - 10.1016/S0008-6215(00)81877-7
DO - 10.1016/S0008-6215(00)81877-7
M3 - Article
C2 - 6458358
AN - SCOPUS:0019882927
SN - 0008-6215
VL - 96
SP - 271
EP - 279
JO - Carbohydrate Research
JF - Carbohydrate Research
IS - 2
ER -