TY - JOUR
T1 - Complete structure of the glycan of lipopeptidophosphoglycan from Trypanosoma cruzi epimastigotes
AU - de Lederkremer, Rosa M.
AU - Lima, Carlos
AU - Ramirez, Maria I.
AU - Ferguson, Michael A. J.
AU - Homans, Steve W.
AU - Thomas-Oates, Jane
PY - 1991/12/15
Y1 - 1991/12/15
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0026334201&partnerID=8YFLogxK
M3 - Article
AN - SCOPUS:0026334201
SN - 0021-9258
VL - 266
SP - 23670
EP - 23675
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 35
ER -