Protein & Peptide Letters

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

DOI: 10.2174/092986608785133744

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

Page: [724 - 730] Pages: 7

  • * (Excluding Mailing and Handling)

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.

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