Hooper N M, Turner A J
Department of Biochemistry, University of Leeds, England.
FEBS Lett. 1988 Mar 14;229(2):340-4. doi: 10.1016/0014-5793(88)81152-9.
The mode of membrane anchorage of three kidney microvillar membrane ectoenzymes has been examined. The release of aminopeptidase P (EC 3.4.11.9) from kidney membranes by bacterial phosphatidylinositol-specific phospholipase C (PI-PLC) and the pattern of detergent solubilization of this ectoenzyme implies that it is anchored to the membrane via a covalently attached glycosyl-phosphatidylinositol moiety. As deduced by phase separation in Triton X-114, octyl-glucoside solubilized the amphipathic form of aminopeptidase P, whereas the PI-PLC-released form displayed hydrophilic properties. In contrast, the pattern of detergent solubilization of two microvillar carboxypeptidases and their resistance to release from the membrane by bacterial PI-PLC suggest that these two ectoenzymes are not anchored via phosphatidylinositol.
三种肾微绒毛膜外切酶的膜锚定方式已被研究。细菌磷脂酰肌醇特异性磷脂酶C（PI-PLC）从肾膜中释放氨肽酶P（EC 3.4.11.9），以及该外切酶的去污剂溶解模式表明，它通过共价连接的糖基磷脂酰肌醇部分锚定在膜上。通过Triton X-114中的相分离推断，辛基葡糖苷溶解了氨肽酶P的两亲形式，而PI-PLC释放的形式表现出亲水性。相比之下，两种微绒毛羧肽酶的去污剂溶解模式及其对细菌PI-PLC从膜上释放的抗性表明，这两种外切酶不是通过磷脂酰肌醇锚定的。
