Purification, biochemical and functional characterization of miliin, a new thiol-dependent serine protease isolated from the latex of Euphorbia milii.

@article{Moro2008PurificationBA,
  title={Purification, biochemical and functional characterization of miliin, a new thiol-dependent serine protease isolated from the latex of Euphorbia milii.},
  author={L P Moro and M{\'a}rio Tyago Murakami and Hamilton Cabral and Alessandra Vidotto and Eloiza Helena Tajara and Raghuvir Krishnaswamy Arni and Luis Juliano and Gustavo Orlando Bonilla-Rodriguez},
  journal={Protein and peptide letters},
  year={2008},
  volume={15 7},
  pages={724-30}
}
Miliin, a new thiol-dependent serine protease purified from the latex of Euphorbia milii possesses a molecular weight of 79 kDa, an isoelectric point of 4.3 and is optimally active at 60 degrees C in the pH range of and 7.5-11.0. Activity tests indicate that milliin is a thiol-dependent serine protease.