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Media type:
E-Article
Title:
Purification and Molecular Cloning of a Major Antibacterial Protein of the Protozoan Parasite Entamoeba Histolytica with Lysozyme‐Like Properties
Description:
<jats:p>A protein with potent antibacterial activity was purified to apparent homogeneity from pathogenic <jats:italic>Entamoeba histolytica.</jats:italic> It resembles lysozyme in that it is a basic protein which degrades cell walls of <jats:italic>Micrococcus luteus</jats:italic>, displays optimal activity at acidic pH, and shows a preference for Gram‐positive bacteria. The protein has a molecular mass of ≈23 kDa upon SDS/PAGE and is localized inside the cytoplasmic granules of the amoebae. The primary structure was elucidated by protein analysis and molecular cloning of the corresponding cDNA. It yielded a protein of 198 residues with structural similarity to the distinct class of lysozymes found in <jats:italic>Streptomyces</jats:italic> species and the fungus <jats:italic>Chalaropsis.</jats:italic></jats:p>