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Purification and Characterization of Mongolian Mare Lactoferrin

  • Published : 2009.04.30

Abstract

The lactoferrin from mongolian mare colostrum has been purified by gel filtration (Sephadex G-100), affinity chromatography (Toyopear1-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 0.5M 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 82kDa. N-terminal amino acid sequence was determined as APRKSVRWCTISPAEXAKXA.

Keywords

References

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