Purification, Biochemical and Functional Characterization of Miliin, a New Thiol-Dependent Serine Protease Isolated from the Latex of Euphorbia milii

Title: Purification, Biochemical and Functional Characterization of Miliin, a New Thiol-Dependent Serine Protease Isolated from the Latex of Euphorbia milii

Volume: 15 Issue: 7

Author(s): L. P. Moro, M. T. Murakami, H. Cabral, A. Vidotto, E. H. Tajara, R. K. Arni, L. Juliano and G. O. Bonilla-Rodriguez

Affiliation:

Keywords: Medicinal plant, Latex, Euphorbia milii, Serine protease, Purification, Characterization

Abstract: 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 °C in the pH range of and 7.5-11.0. Activity tests indicate that milliin is a thiol-dependent serine protease.

Cite this article as:

Moro P. L., Murakami T. M., Cabral H., Vidotto A., Tajara H. E., Arni K. R., Juliano L. and Bonilla-Rodriguez O. G., Purification, Biochemical and Functional Characterization of Miliin, a New Thiol-Dependent Serine Protease Isolated from the Latex of Euphorbia milii, Protein & Peptide Letters 2008; 15 (7) . https://dx.doi.org/10.2174/092986608785133744