MOLECULAR CHARACTERIZATION OF AN EXCEPTIONALLY ACIDIC LYSOZYME-LIKE PROTEIN FROM THE PROTOZOAN ENTAMOEBA-HISTOLYTICA

Citation
R. Nickel et al., MOLECULAR CHARACTERIZATION OF AN EXCEPTIONALLY ACIDIC LYSOZYME-LIKE PROTEIN FROM THE PROTOZOAN ENTAMOEBA-HISTOLYTICA, FEBS letters, 437(1-2), 1998, pp. 153-157
Citations number
22
Categorie Soggetti
Biology,"Cell Biology",Biophysics
Journal title
ISSN journal
00145793
Volume
437
Issue
1-2
Year of publication
1998
Pages
153 - 157
Database
ISI
SICI code
0014-5793(1998)437:1-2<153:MCOAEA>2.0.ZU;2-X
Abstract
The protozoan parasite Entamoeba histolytica contains a second antibac terial protein with lysozyme-like properties. The newly recognized bac teriolytic protein was purified from extracts of amoebic trophozoites to allow amino-terminal sequencing. Subsequent molecular cloning revea led that it is an isoform of the amoeba lysozyme described previously but also demonstrated a substantial sequence divergence of the two for ms. As lysozymes typically are basic proteins, the novel amoebic prote in differs markedly in having a pI of 4.5. There is no significant sim ilarity of both amoeba lysozymes with any bacteriolytic protein of oth er organisms reported so far; however, striking sequence identity is f ound with predicted gene products of unknown function derived from the bacteria-feeding nematode Caenorhabditis elegans. (C) 1998 Federation of European Biochemical Societies.