Shafit-Zagardo B, Turner B M
Biochim Biophys Acta. 1981 May 14;659(1):7-14. doi: 10.1016/0005-2744(81)90265-5.
The acid beta-glucosidase (D-glucosyl-N-acylsphingosine glucohydrolase, EC 3.2.1.45) from human placenta is inhibited by sulphated macromolecules such as Dextran sulphate or chondroitin sulphate. This inhibition is alleviated by compounds such as crude taurocholate or phospholipids, which are known activators of acid beta-glucosidase. Partially-purified human beta-glucosidase will bind to Dextran sulphate linked to Sepharose 4B and can be eluted with low concentrations of crude sodium taurocholate. This procedure gives a 10-15 fold purification with good yield and has been included in a scheme giving an approx. 4000-fold purification of placental beta-glucosidase. Evidence is presented which suggests that phospholipids bind to beta-glucosidase by both ionic and hydrophobic interactions. The inhibition of enzyme activity caused by sulphated compounds and non-ionic detergents may be attributed to interference with, respectively, the ionic and hydrophobic binding of phospholipid to the enzyme.
人胎盘来源的酸性β-葡萄糖苷酶（D-葡萄糖基-N-酰基鞘氨醇葡萄糖水解酶，EC 3.2.1.45）会受到硫酸化大分子如硫酸葡聚糖或硫酸软骨素的抑制。这种抑制作用可被粗制牛磺胆酸盐或磷脂等化合物缓解，这些化合物是已知的酸性β-葡萄糖苷酶激活剂。部分纯化的人β-葡萄糖苷酶会与连接到琼脂糖4B上的硫酸葡聚糖结合，并能用低浓度的粗制牛磺胆酸钠洗脱。该方法可实现10至15倍的纯化，产率良好，且已被纳入一个能使胎盘β-葡萄糖苷酶实现约4000倍纯化率的方案中。有证据表明，磷脂通过离子相互作用和疏水相互作用与β-葡萄糖苷酶结合。硫酸化化合物和非离子型去污剂对酶活性的抑制作用可能分别归因于它们对磷脂与酶的离子结合和疏水结合的干扰。
