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In this work, we report the partial sequence of a 51 kDa protein of Entamoeba histolytica that is highly immunogenic in humans. Partial sequencing of the N-terminal end showed that 18 of the first 20 amino acid residues of the protein were identified uniquely, indicating that the final product was a homogeneous protein preparation. The N-terminal sequence that was found was: KVYFEETFENGWKXIWSKW. Comparing the 19-amino acid sequence of the protein in automated databases shows significant similarity with amino acid sequences of the calreticulin-like protein of spinach leaves (77%) and of the calreticulin precursor of Dictyostelium discoideum (60%).
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G. C. McGugan Jr., M. B. Joshi, and D. M. Dwyer Identification and Biochemical Characterization of Unique Secretory Nucleases of the Human Enteric Pathogen, Entamoeba histolytica J. Biol. Chem., October 26, 2007; 282(43): 31789 - 31802. [Abstract] [Full Text] [PDF] |
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