Di Natale P, Murino P, Pontarelli G, Salvatore D, Andria G
Clin Chim Acta. 1982 Jul 1;122(2):135-43. doi: 10.1016/0009-8981(82)90273-x.
We studied the residual alpha-N-acetylglucosaminidase activity in two siblings with severe and mild Sanfilippo B syndrome. No striking differences were demonstrated between the mutant enzymes from the severe and the mild case. However we found an altered enzyme activity characterized by displacement of the pH optimum towards basic values compared to the pH optimum of the normal enzyme, higher stability to heat and to Hg2+ ion treatment. It is suggested that the Sanfilippo B disease in this sibship is due to a mutation of a structural gene coding for alpha-N-acetylglucosaminidase.
我们研究了两名患有重度和轻度桑菲利波B综合征的同胞中残余的α-N-乙酰氨基葡萄糖苷酶活性。重度和轻度病例的突变酶之间未显示出明显差异。然而,我们发现该酶活性发生了改变,其特征是与正常酶的最适pH值相比,最适pH值向碱性值偏移,对热和Hg2+离子处理具有更高的稳定性。提示该同胞中的桑菲利波B病是由于编码α-N-乙酰氨基葡萄糖苷酶的结构基因突变所致。