| Literature DB >> 3011506 |
Y Takesue, K Yokota, Y Nishi, R Taguchi, H Ikezawa.
Abstract
Trehalase (EC 3.2.1.28) associated with renal and intestinal brush-border membranes was solubilized by highly purified phosphatidylinositol-specific phospholipase C (EC 3.1.4.10) from Bacillus thuringiensis, but not by phosphatidylcholine-hydrolyzing phospholipase C (EC 3.1.4.3) from Clostridium welchii or phospholipase D (EC 3.1.4.4) from cabbage. The solubilized trehalase was not adsorbed on phenyl-Sepharose, indicating that it was hydrophilic. Phosphatidylinositol-specific phospholipase C also converted Triton X-100-solubilized amphipathic trehalase into a hydrophilic form. These results suggest that trehalase is bound to the membrane through a direct and specific interaction with phosphatidylinositol.Entities:
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Year: 1986 PMID: 3011506 DOI: 10.1016/0014-5793(86)80560-9
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124