title: Purification of camel milk lysozyme and its lytic effect on Escherichia coli and Micrococcus lysodeikticus.
abstract: 1. Camel milk lysozyme was purified using heparin-Sepharose 4B, Sephadex G-75 and hydroxyapatite chromatography. By this procedure lysozyme was separated from lactoferrin and a low molecular weight protein. 2. The lytic effect of camel milk lysozyme was assayed using Escherichia coli and Micrococcus lysodeikticus and its activity was compared with that of lysozyme from human milk and egg white. 3. The specific activity of camel milk lysozyme was found to be lower than that of lysozyme from human milk or from egg white. 4. Camel milk lactoferrin did not show a lytic effect on bacteria, while the low molecular weight protein showed lytic activity.
authors.affiliation: Department of Biochemistry, College of Science, King Saud University, Riyadh, Saudi Arabia.
authors.forename: A S
authors.initials: AS
authors.lastname: Duhaiman
mesh_terms: D000818:Animals; D002162:Camelus / Q000378:metabolism*; D004527:Egg Proteins / Q000302:isolation & purification; D004926:Escherichia coli / Q000187:drug effects; D005260:Female; D006801:Humans; D007781:Lactoferrin / Q000302:isolation & purification; D008837:Micrococcus / Q000187:drug effects; D008892:Milk / Q000201:enzymology*; D008895:Milk, Human / Q000201:enzymology; D008970:Molecular Weight; D009113:Muramidase / Q000302:isolation & purification* / Q000494:pharmacology
chemical_list: D004527:Egg Proteins; D009113:Muramidase; D007781:Lactoferrin