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Title: Characterization of the phosphatidylinositol-glycan membrane anchor of human placental alkaline phosphatase

Journal Article · · Proc. Natl. Acad. Sci. U.S.A.; (United States)

Placental alkaline phosphatase (orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1) is a member of a diverse group of membrane proteins whose attachment to the lipid bilayer is mediated by a phosphatidylinositol-glycan. To investigate structural aspects of the glycolipid anchor, cultured WISH cells were used because, they produce the enzyme in abundant quantities. When cell suspensions were incubated with purified phosphatidylinositol-specific phospholipase C, most of the placental alkaline phosphatase was released from membranes in a hydrophilic form. On incubation of the cells with (/sup 14/C)ethanolamine, (/sup 14/C)myristic acid, or myo(/sup 3/H)inositol, each was incorporated into the phosphatase near the carboxyl terminus, showing that these components, which are found in other phosphatidylinositol membrane-linked proteins, are also present in placental alkaline phosphatase.

Research Organization:
Roche Research Center, Nutley, NJ (USA)
OSTI ID:
5175508
Journal Information:
Proc. Natl. Acad. Sci. U.S.A.; (United States), Vol. 84:17
Country of Publication:
United States
Language:
English

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