Site of palmitoylation of a phospholipase C-resistant glycosyl-phosphatidylinositol membrane anchor

The site of palmitoylation of the phosphatidylinositol moiety of the glycosyl-phosphatidylinositol membrane anchor of Trypanosoma brucei procyclic repetitive protein was studied by using periodate oxidation. Analysis of the products by g.c.-m.s. allowed the assignment of 40 and 60% of the palmitate...

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Bibliographic Details
Published in:	Biochemical journal Vol. 284; no. 2; pp. 297 - 300
Main Author:	FERGUSON, M. A. J
Format:	Journal Article
Language:	English
Published:	Colchester Portland Press 1992
Subjects:	Analytical, structural and metabolic biochemistry Biological and medical sciences cell membranes Fundamental and applied biological sciences. Psychology Glycoproteins glycosylphosphatidylinositol identification incorporation palmitic acid procyclic acidic repetitive protein Proteins sites Trypanosoma brucei Protozoa Phosphatidylinositol Plasma membrane Rhizoflagellata Glycoproteins Palmitic acid Trypanosoma brucei Anchoring Acylation
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Summary:	The site of palmitoylation of the phosphatidylinositol moiety of the glycosyl-phosphatidylinositol membrane anchor of Trypanosoma brucei procyclic repetitive protein was studied by using periodate oxidation. Analysis of the products by g.c.-m.s. allowed the assignment of 40 and 60% of the palmitate to the 2-position and the 3-position respectively of the myo-inositol ring.
Bibliography:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23
ISSN:	0264-6021 1470-8728
DOI:	10.1042/bj2840297