Toma S, Coppa G, Donnelly P V, Ricci R, Di Ferrante N, Srivastava S K
Carbohydr Res. 1981 Oct 16;96(2):271-90. doi: 10.1016/s0008-6215(00)81877-7.
The disaccharide 2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1 goes to 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, effective degradation of keratan sulfate, secondary to a defect of the beta subunits present in the A and B isoenzymes of hexosaminidase, may contribute to the appearance of skeletal lesions in patients affected by Sandhoff disease.
由硫酸角质素制备的二糖2-乙酰氨基-2-脱氧-β-D-吡喃葡萄糖基-(1→3)-D-[1-³H]-半乳糖醇，可被正常人肝脏己糖胺酶（EC 3.2.1.30）的A和B同工酶以及死于泰-萨克斯病患者肝脏中制备的B同工酶迅速水解。该二糖底物也可被正常培养的皮肤成纤维细胞提取物以及泰-萨克斯病患者的成纤维细胞水解，而桑德霍夫病患者的成纤维细胞提取物则不能水解该底物。因此，由于己糖胺酶A和B同工酶中β亚基缺陷导致的硫酸角质素有效降解，可能是桑德霍夫病患者骨骼病变出现的原因之一。
