Savolainen H
Biochem J. 1976 Mar 1;153(3):749-50. doi: 10.1042/bj1530749.
The isolation of liver N-aspartyl-beta-glucosaminidase in human aspartylglucosaminuria, where this enzyme activity is diminished, yields an enzyme molecule with the same molecular weight and pH optimum as the normal enzyme. Its activity is 10% of that of the control preparation. Combination of both enzymes results in the summation of both activities, and the pathological enzyme does not inhibit the control preparation. It is concluded that no change into a totally different isoenzyme has occurred in aspartylglucosaminuria.
在天冬氨酰葡糖胺尿症患者中，肝脏N-天冬氨酰-β-葡糖胺酶活性降低，分离得到的该酶分子与正常酶具有相同的分子量和最适pH值。其活性为对照制剂的10%。两种酶结合后，活性相加，病理性酶并不抑制对照制剂。由此得出结论，在天冬氨酰葡糖胺尿症中并未发生向完全不同的同工酶的转变。
