title: Renal dipeptidase is one of the membrane proteins released by phosphatidylinositol-specific phospholipase C.
abstract: 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.
authors.affiliation: Department of Biochemistry, University of Leeds, U.K.
authors.forename: N M
authors.initials: NM
authors.lastname: Hooper
authors.forename: M G
authors.initials: MG
authors.lastname: Low
authors.forename: A J
authors.initials: AJ
authors.lastname: Turner
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000187:drug effects / Q000201:enzymology; D015377:Cilastatin; D003521:Cyclopropanes / Q000494:pharmacology; D004150:Dipeptidases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D007668:Kidney / Q000187:drug effects / Q000201:enzymology*; D008565:Membrane Proteins / Q000378:metabolism*; D043265:Phosphatidylinositol Diacylglycerol-Lyase; D054801:Phosphoinositide Phospholipase C; D010727:Phosphoric Diester Hydrolases / Q000378:metabolism*; D011092:Polyethylene Glycols / Q000494:pharmacology; D013552:Swine
chemical_list: D003521:Cyclopropanes; D008565:Membrane Proteins; D015377:Cilastatin; D011092:Polyethylene Glycols; D010727:Phosphoric Diester Hydrolases; D054801:Phosphoinositide Phospholipase C; D004150:Dipeptidases; C038937:dipeptidase; D043265:Phosphatidylinositol Diacylglycerol-Lyase