doi: 10.1111/j.1432-1033.1995.0831d.x.
Purification and molecular cloning of a major antibacterial protein of the protozoan parasite Entamoeba histolytica with lysozyme-like properties
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- PMID: 7649184
- DOI: 10.1111/j.1432-1033.1995.0831d.x
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Purification and molecular cloning of a major antibacterial protein of the protozoan parasite Entamoeba histolytica with lysozyme-like properties
Eur J Biochem.
.
Free article
Abstract
A protein with potent antibacterial activity was purified to apparent homogeneity from pathogenic Entamoeba histolytica. It resembles lysozyme in that it is a basic protein which degrades cell walls of Micrococcus luteus, displays optimal activity at acidic pH, and shows a preference for Gram-positive bacteria. The protein has a molecular mass of approximately 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 Streptomyces species and the fungus Chalaropsis.
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