Purification of anticoagulant peptides derived from egg white powder

The anticoagulant peptides derived from egg white powder were hydrolysised by Alcalase and then purified by SephadexG-50 and semi-preparative reversed phaseliquid chromatography (RPLC). High activity fraction was selected after rotary evaporation and freeze drying. The anticoagulant activity was determined by micro plate reader. The results showed that the No.4 fraction of eluted by SephadexG-50 at time 35~40 min had high anticoagulant activities which were 84.74%. Then, this fraction was purified by semi-preparative reversed phaseliquid chromatography in which it separated to 12 peaks. Peak VII was eluted at 17.275~19.542 min. The highest anticoagulant activities of fractions was peak VII which inhibition rate reached up to 71.27%.