Abstract

Human and bovine lactoferrin have been studied extensively, but very few reports exist on camel (Camelus dromedarius) lactoferrin. This iron-binding glycoprotein is present primarily in milk. It has been shown to be involved in various physiological and protective functions, including homeostasis and cell proliferation, and it has antibacterial, antifungal, antiviral, antioxidant, immunomodulatory and anticancer activities. This study aimed to compare the protein profiles of camel milk and bovine milk by gel electrophoresis and to isolate camel lactoferrin from colostrum. Camel milk proteins profile lacked β-lactoglobulin. Lactoferrin was isolated from colostrum by cation exchange chromatography and identified by its molecular weight after gel electrophoresis as a single band of about 78 kDa, demonstrating the purity of the isolated protein. The study demonstrates a simple one-step method to purify lactoferrin from camel colostrum.

Key words: Lactoferrin (Lf), Camel Lactoferrin (CLf), Colostrum, Cation Exchange Chromatography (CEC)