Purification and Characterization of Mongolian Mare Lactoferrin

The lactoferrin from mongolian mare colostrum has been purified by gel filtration (Sephadex G-100), affinity chromatography (Toyopearl-AF-Heparin-650M) in two steps. Mare lactoferrin-containing fractions were identified in the first peak among 3 peaks on Sephadex G-100 as first step, and purified lactoferrin was eluted with a step gradient of 0.5 M NaCl as a 3 step (gradient 0.1, 0.3, 0.5M). Eluted fractions were analyzed by 12% SDS-PAGE, and showed a single protein. Its molecular weight was estimated to be 82 kDa. N-terminal amino acid sequence was determined as APRKSVRWCTISPAEX-AKXA.