Renal dipeptidase (dehydropeptidase-I, EC 18.104.22.168) 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.
Research Article| June 01 1987
Renal dipeptidase is one of the membrane proteins released by phosphatidylinositol-specific phospholipase C.
N M Hooper;
M G Low;
Biochem J (1987) 244 (2): 465–469.
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N M Hooper, M G Low, A J Turner; Renal dipeptidase is one of the membrane proteins released by phosphatidylinositol-specific phospholipase C.. Biochem J 1 June 1987; 244 (2): 465–469. doi: https://doi.org/10.1042/bj2440465
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