| Literature DB >> 15955316 |
James J McCoy1, Barbara J Mann.
Abstract
Contact-dependent killing and phagocytosis of target cells by Entamoeba histolytica trophozoites is mediated by the galactose (Gal) and N-acetyl-d-galactosamine (GalNAc)-inhibitable lectin. Previous work has suggested that this lectin functions as part of a signal transduction complex. To identify proteins that might be part of this complex, amebic trophozoites were bound to GalNAc-BSA-labeled magnetic beads and lysed. Bound proteins were eluted from the beads and analyzed by tandem mass spectrometry. Along with the Gal/GalNAc lectin subunits, several cytoskeletal proteins, potential signaling proteins, and a novel transmembrane protein, consistently purified with the GalNAc-BSA beads.Entities:
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Year: 2005 PMID： 15955316 DOI： 10.1016/j.exppara.2005.02.013
Source DB: PubMed Journal: Exp Parasitol ISSN： 0014-4894 Impact factor: 2.011