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    Science. 1991 Apr 19;252(5004):446-8.

    Primary structure and functional activity of a phosphatidylinositol-glycan-specific phospholipase D.

    Scallon BJ, Fung WJ, Tsang TC, Li S, Kado-Fong H, Huang KS, Kochan JP.

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    Department of Molecular/Cellular Biology and Biochemistry, Hoffmann-La Roche, Inc., Nutley, NJ 07110.

    Abstract

    A phosphatidylinositol-glycan-specific phospholipase D (PI-G PLD) that specifically hydrolyzes the inositol phosphate linkage in proteins anchored by phosphatidylinositol-glycans (PI-Gs) has recently been purified from human and bovine sera. The primary structure of bovine PI-G PLD has now been determined and the functional activity of the enzyme has been studied. Expression of PI-G PLD complementary DNA in COS cells produced a protein that specifically hydrolyzed the inositol phosphate linkage of the PI-G anchor. Cotransfection of PI-G PLD with a PI-G-anchored protein resulted in the secretion of the PI-G-anchored protein. The results suggest that the expression of PI-G PLD may influence the expression and location of PI-G-anchored proteins.

    PMID:
    2017684
    [PubMed - indexed for MEDLINE]

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