Ectoenzymes of the kidney microvillar membrane Aminopeptidase P is anchored by a glycosyl‐phosphatidylinositol moiety

FEBS Letters

Hooper, Nigel M.¹  Turner, Anthony J.¹ 

[1] MRC Membrane Peptidase Research Group, Department of Biochemistry, University of Leeds, Leeds LS2 9JT, England

关键词: Aminopeptidase P;    Ectoenzyme;    Carboxypeptidase;    Glycosyl-phosphatidylinositol;    Membrane anchor;    CHAPS;    3-[3-cholamidopropyl)dimethylammonio]-1-propane sulphonate;    CMC;    critical micellar concentration;    octyl-glucoside;    n-octyl-β-D-glucopyranoside;    PI;    phosphatidylinositol;    PI-PLC;    phosphatidylinositol-specific phospholipase C;   

DOI  :  10.1016/0014-5793(88)81152-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown