Solubilization of trehalase from rabbit renal and intestinal brush‐border membranes by a phosphatidylinositol‐specific phospholipase C

FEBS Letters

Taguchi, Ryo²  Ikezawa, Hiroh²  Yokota, Kunio¹  Nishi, Yoshimi³  Takesue, Yoshiki¹ 

[1] Research Institute of Environmental Medicine, Nagoya University, Chikusa-ku, Nagoya 464 Japan;Faculty of Pharmaceutical sciences, Nagoya City University, Mizuho-ku, Nagoya 467, Japan;Aichi Cancer Center Research Institute, Chikusa-ku, Nagoya 464 Japan

关键词: Trehalase;    Phosphatidylinositol specificity;    Phospholipase C;    Brush-border membrane;    Alkaline phosphatase;    Endopeptidase;    PIPLC;    phosphatidylinositol-specific phospholipase C;    BBM;    brush-border membrane;   

DOI  :  10.1016/0014-5793(86)80560-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown