Moro, L. P. [UNESP]Murakami, M. T.Cabral, Hamilton [UNESP]Vidotto, A.Tajara, E. H.Arni, R. K. [UNESP]Juliano, L.Bonilla-Rodriguez, Gustavo Orlando [UNESP]2014-05-202014-05-202008-07-01Protein and Peptide Letters. Sharjah: Bentham Science Publ Ltd, v. 15, n. 7, p. 724-730, 2008.0929-8665http://hdl.handle.net/11449/22025Miliin, 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.724-730engMedicinal plantlatexEuphorbia miliiserine proteasePurificationCharacterizationPurification, biochemical and functional characterization of miliin, a new thiol-dependent serine protease isolated from the latex of Euphorbia miliiArtigoWOS:000259509600012Acesso restrito916250897894588769552585886721300000-0003-2460-1145