Dugal B
Biochem J. 1977 Apr 1;163(1):9-14. doi: 10.1042/bj1630009.
The activity of 1-aspartamido-beta-N-acetylglucosamine amidohydrolase (aspartylglucosylaminase, EC 3.5.1.26) was measured in normal and diseased human liver, brain and kidney. Organs from patients with aspartylglucosaminuria show very little activity. Crude homogenates of human organs show a reaction catalysed by a complex enzyme system. With homogenate, the formation of product was linear with time up to about 6 h. Reaction times longer than 6-7h resulted in a decrease in the total concentration of product. This phenomenon was not found with the partially purified enzyme fraction. Linearity of the enzyme activity with different protein concentrations was found, independent of the incubation time. Longer incubation of the crude homogenate resulted in the utilization of the product, N-acetylglucosamine. This phenomenon was not observed with the partially purified enzyme fraction. This amidase from human organs differs from that obtained from other sources and apparently represents a rather complex enzyme system.
在正常和患病的人类肝脏、大脑及肾脏中测量了1-天冬氨酰-β-N-乙酰葡糖胺酰胺水解酶（天冬氨酰葡糖胺酶，EC 3.5.1.26）的活性。患有天冬氨酰葡糖胺尿症患者的器官显示出极低的活性。人类器官的粗匀浆显示出由一个复合酶系统催化的反应。对于匀浆，产物的形成在长达约6小时内与时间呈线性关系。反应时间超过6 - 7小时会导致产物总浓度降低。在部分纯化的酶组分中未发现此现象。发现酶活性与不同蛋白质浓度呈线性关系，与孵育时间无关。粗匀浆孵育时间延长会导致产物N-乙酰葡糖胺的消耗。在部分纯化的酶组分中未观察到此现象。来自人类器官的这种酰胺酶与从其他来源获得的不同，显然代表了一个相当复杂的酶系统。
