Abstract
The lipopeptidophosphoglycan is the major cell surface glycoconjugate of the epimastigote forms of the parasitic protozoan Trypanosoma cruzi. A detailed partial structure for this molecule has been reported (Previato, J.O., Gorin, P.A.J., Mazurek, M., Xavier, M.T., Fournet, B., Wieruszesk, J.M., and Mendonca-Previato, L. (1990) J. Biol. Chem. 265, 2518-2526). In this study, we complete the primary structure assignments and describe the microheterogeneity found in the lipopeptidophosphoglycan glycan, using a combination of 1H and 31P NMR, fast atom bombardment mass spectrometry, methylation linkage analysis, and exoglycosidase sequencing. The lipopeptidophosphoglycan is a glycosylated inositol-phosphoceramide with striking homology to glycosylphosphatidylinositol membrane anchors found attached to a wide variety of membrane anchors found attached to a wide variety of plasma membrane proteins throughout the eukaryotes.
| Original language | English |
|---|---|
| Pages (from-to) | 23670-23675 |
| Number of pages | 6 |
| Journal | Journal of Biological Chemistry |
| Volume | 266 |
| Issue number | 35 |
| Publication status | Published - 15 Dec 1991 |
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