A SIMPLE PURIFICATION OF PROCYCLIC ACIDIC REPETITIVE PROTEIN AND DEMONSTRATION OF A SIALYLATED GLYCOSYL-PHOSPHATIDYLINOSITOL MEMBRANE ANCHOR
- Author(s)
- FERGUSON, MAJ; MURRAY, P; RUTHERFORD, H; McConville, MJ;
- Journal Title
- BIOCHEMICAL JOURNAL
- Publication Type
- Journal Article
- Abstract
- The procyclic acidic repetitive protein is the major cell-surface glycoprotein of the insect-dwelling procyclic forms of the Trypanosoma brucei species of African trypanosomes. The glycoprotein contains an acidic Glu-Pro repeat domain, a glycosyl-phosphatidylinositol membrane anchor and a putative asparagine glycosylation site. In this paper we describe a rapid purification scheme for this glycoprotein, using solvent extraction and hydrophobic interaction chromatography, and a partial characterization of the glycosylphosphatidylinositol membrane anchor. The carbohydrate composition of the anchor is extremely unusual; it contains on average nine GlcNAc, nine Gal and five sialic acid residues. This is the first description of such a heavily substituted and negatively charged anchor. A comparison between the trypanosome procyclic surface and the Leishmania promastigote surface is also presented.
- Publisher
- PORTLAND PRESS
- Keywords
- VARIANT SURFACE GLYCOPROTEIN; ASPARAGINE-LINKED OLIGOSACCHARIDES; TRYPANOSOMA-BRUCEI; LEISHMANIA-MAJOR; AFRICAN TRYPANOSOMES; SIALIC-ACID; STAGE; LIPOPHOSPHOGLYCAN; GLYCOLIPIDS; EXPRESSION
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Creation Date: 1993-04-01 12:00:00