Publication Date:
1991-04-19
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scallon, B J -- Fung, W J -- Tsang, T C -- Li, S -- Kado-Fong, H -- Huang, K S -- Kochan, J P -- New York, N.Y. -- Science. 1991 Apr 19;252(5004):446-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular/Cellular Biology and Biochemistry, Hoffmann-La Roche, Inc., Nutley, NJ 07110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2017684" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Animals
;
Cattle
;
Cell Line
;
Cloning, Molecular
;
DNA/genetics
;
Gene Expression
;
Glycosylphosphatidylinositols
;
Humans
;
Hydrolysis
;
Molecular Sequence Data
;
Peptide Fragments/chemistry
;
Phosphatidylinositols/metabolism
;
Phospholipase D/*chemistry/genetics/metabolism
;
Polysaccharides/metabolism
;
Sequence Homology, Nucleic Acid
;
Transfection
;
Trypsin
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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