Lactoferrin (LF) is a Fe3+-binding glycoprotein, that was first recognized in milk and then in other epithelial secretions and barrier body fluids to which many different functions have been attributed to LF including protection from iron-induced lipid peroxidation, immunomodulation, cell growth regulation, DNA and RNA binding, as well as transcriptional activation, еtс. The polyfunctional physiological role of LF is still unclear, but it has been suggested to be responsible for primary defense against microbial and viral infections. It was shown previously that human milk LF possesses several enzymatic activities: DNase, RNase, ATPase, phosphatase, and amylase. Analysis of human, cow, horse, buffalo and camel LF showed a highly conserved three-dimensional (3D) structure including only detail differences in the species. Recently, it was shown that similar to human cow LF possesses DNase and RNase activities. Using different methods here we have shown for the first time that LFs from the milk of seven cows of different breeds possess high peroxidase, protease, amylase, protease, and phosphatase activities. Protease activity of cow LFs was activated by Mg2+ and Ca2+ ions. In contrast to human LFs, ATPase activity was revealed only in three of seven cow LF preparations. The discovery that LF possesses these activities may contribute to understanding the multiple physiological functions of this extremely polyfunctional protein including its protective role against microbial and viral infections.
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