Radin N S, Shukla A, Shukla G S, Sano A
Mental Health Research Institute, University of Michigan, Ann Arbor 48104.
Biochem J. 1989 Dec 15;264(3):845-9. doi: 10.1042/bj2640845.
A hot-water extract of bovine spleen and guinea pig liver exhibited the ability to enhance acid alpha-glucosidase activity, with methylumbelliferyl alpha-glucoside, glycogen or maltose as substrate. The level of activator required for maximal stabilization was similar for all three substrates, indicating direct action on the enzyme rather than on substrate. The stimulator was partially purified by chromatography with gel-permeation (apparent Mr 20,000-24,000), ion-exchange and C4 reverse-phase columns. It was retained by a narrow-pore dialysis tubing and destroyed by treatment with Pronase, and is presumably a protein. The stimulating protein protected the enzyme against denaturation by heat or incubation with a buffer of high ionic strength in the absence of substrate. RNA inhibited the enzyme, and the activator protein was able to counteract the effect. Activating material was found in a variety of mouse and rat tissues, as well as human urine.
牛脾和豚鼠肝脏的热水提取物能够增强酸性α-葡萄糖苷酶的活性，以甲基伞形酮基α-葡萄糖苷、糖原或麦芽糖作为底物。对于所有三种底物，实现最大程度稳定所需的激活剂水平相似，这表明其直接作用于酶而非底物。通过凝胶渗透（表观分子量为20,000 - 24,000）、离子交换和C4反相柱色谱法对刺激物进行了部分纯化。它能被窄孔透析管截留，经链霉蛋白酶处理后被破坏，推测是一种蛋白质。这种刺激蛋白可保护酶免受热变性或在无底物情况下与高离子强度缓冲液孵育时的变性。RNA会抑制该酶，而激活蛋白能够抵消这种作用。在多种小鼠和大鼠组织以及人类尿液中均发现了激活物质。
