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Science 19 April 1991: Vol. 252. no. 5004, pp. 446 - 448 DOI: 10.1126/science.2017684
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Articles
Science, Vol 252, Issue 5004, 446-448
Copyright © 1991 by American Association for the Advancement of Science
Primary structure and functional activity of a phosphatidylinositol-glycan-specific phospholipase D
BJ Scallon,
WJ Fung,
TC Tsang,
S Li,
H Kado-Fong,
KS Huang,
and
JP Kochan
Department of Molecular/Cellular Biology and Biochemistry, Hoffmann-La Roche, Inc., Nutley, NJ 07110.
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.
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