Purification and characterization of a Kunitz-type trypsin inhibitor from Acacia victoriae Bentham seeds.

@article{Ee2009PurificationAC,
  title={Purification and characterization of a Kunitz-type trypsin inhibitor from Acacia victoriae Bentham seeds.},
  author={K. Y. Ee and Jian M. Zhao and Ata-ur Rehman and Samson O Agboola},
  journal={Journal of agricultural and food chemistry},
  year={2009},
  volume={57 15},
  pages={7022-9}
}
An Acacia victoriae trypsin inhibitor (AvTI) was purified from the seeds of prickly wattle (A. victoriae Bentham) by salt precipitation, ion exchange, and gel filtration chromatography and then characterized by electrophoresis and N-terminal amino acid sequencing. AvTI had a specific activity of 138.99 trypsin inhibitor units per milligram (TIU mg(-1)), which was 21-fold higher than that of the salt precipitate. A molecular mass of 13 kDa was estimated by sodium dodecyl sulfate-polyacrylamide… CONTINUE READING