Structure of the glycosyl-phosphatidylinositol membrane anchor of the Leishmania major promastigote surface protease.

@article{Schneider1990StructureOT,
  title={Structure of the glycosyl-phosphatidylinositol membrane anchor of the Leishmania major promastigote surface protease.},
  author={Polin Schneider and Michael A J Ferguson and Malcolm J. McConville and Angela Mehlert and Steven W. Homans and Christine Bordier},
  journal={The Journal of biological chemistry},
  year={1990},
  volume={265 28},
  pages={
          16955-64
        }
}
In common with many other plasma membrane glycoproteins of eukaryotic origin, the promastigote surface protease (PSP) of the protozoan parasite Leishmania contains a glycosyl-phosphatidylinositol (GPI) membrane anchor. The GPI anchor of Leishmania major PSP was purified following proteolysis of the PSP and analyzed by two-dimensional 1H-1H NMR, compositional and methylation linkage analyses, chemical and enzymatic modifications, and amino acid sequencing. From these results, the structure of… CONTINUE READING

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