Hooper N M, Low M G, Turner A J
Department of Biochemistry, University of Leeds, U.K.
Biochem J. 1987 Jun 1;244(2):465-9. doi: 10.1042/bj2440465.
Renal dipeptidase (dehydropeptidase-I, EC 3.4.13.11) was released from pig kidney membrane preparations by treatment with phosphatidylinositol-specific phospholipase C from Staphylococcus aureus and Bacillus thuringiensis and a phospholipase C preparation from Bacillus cereus to a similar extent as alkaline phosphatase. Endopeptidase-24.11 and aminopeptidase N were not released by this treatment. After treatment of the membrane fraction with the S. aureus phospholipase C the dipeptidase was converted from an amphipathic to a hydrophilic form, as deduced from phase-separation experiments in Triton X-114. It is concluded that renal dipeptidase is anchored to the microvillar membrane by covalently attached phosphatidylinositol.
用来自金黄色葡萄球菌、苏云金芽孢杆菌的磷脂酰肌醇特异性磷脂酶C以及蜡状芽孢杆菌的磷脂酶C制剂处理猪肾膜制剂,肾二肽酶(脱氢肽酶-I,EC 3.4.13.11)的释放程度与碱性磷酸酶相似。这种处理不会释放内肽酶-24.11和氨肽酶N。用金黄色葡萄球菌磷脂酶C处理膜部分后,根据Triton X-114中的相分离实验推断,二肽酶从两亲形式转变为亲水形式。得出的结论是,肾二肽酶通过共价连接的磷脂酰肌醇锚定在微绒毛膜上。