| Literature DB >> 2822007 |
N M Hooper1, M G Low, A J Turner.
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.Entities:
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Year: 1987 PMID: 2822007 PMCID: PMC1148013 DOI: 10.1042/bj2440465
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857