Purification, biochemical and functional characterization of miliin, a new thiol-dependent serine protease isolated from the latex of Euphorbia milii
dc.contributor.author | Moro, L. P. [UNESP] | |
dc.contributor.author | Murakami, M. T. | |
dc.contributor.author | Cabral, Hamilton [UNESP] | |
dc.contributor.author | Vidotto, A. | |
dc.contributor.author | Tajara, E. H. | |
dc.contributor.author | Arni, R. K. [UNESP] | |
dc.contributor.author | Juliano, L. | |
dc.contributor.author | Bonilla-Rodriguez, Gustavo Orlando [UNESP] | |
dc.contributor.institution | Universidade Estadual Paulista (Unesp) | |
dc.contributor.institution | Ctr Struct Mol Biol | |
dc.contributor.institution | Universidade de São Paulo (USP) | |
dc.contributor.institution | Faculdade de Medicina de São José do Rio Preto (FAMERP) | |
dc.contributor.institution | Universidade Federal de São Paulo (UNIFESP) | |
dc.date.accessioned | 2014-05-20T14:02:29Z | |
dc.date.available | 2014-05-20T14:02:29Z | |
dc.date.issued | 2008-07-01 | |
dc.description.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 degrees C in the pH range of and 7.5-11.0. Activity tests indicate that milliin is a thiol-dependent serine protease. | en |
dc.description.affiliation | UNESP, IBILCE, DQCA, Dept Chem & Environm Sci, BR-15054000 Sao Jose do Rio Preto, SP, Brazil | |
dc.description.affiliation | UNESP, IBILCE, Mol Biophys Grad Program, BR-15054000 Sao Jose do Rio Preto, SP, Brazil | |
dc.description.affiliation | Ctr Struct Mol Biol, Campinas, SP, Brazil | |
dc.description.affiliation | Univ São Paulo, Fac Pharm, BR-14049 Ribeirao Preto, SP, Brazil | |
dc.description.affiliation | FAMERP, Dept Mol Biol, Sao Jose do Rio Preto, SP, Brazil | |
dc.description.affiliation | UNESP, IBILCE, Dept Phys, BR-15054000 Sao Jose do Rio Preto, SP, Brazil | |
dc.description.affiliation | Univ Fed São Paulo, Dept Biophys, São Paulo, Brazil | |
dc.description.affiliationUnesp | UNESP, IBILCE, DQCA, Dept Chem & Environm Sci, BR-15054000 Sao Jose do Rio Preto, SP, Brazil | |
dc.description.affiliationUnesp | UNESP, IBILCE, Mol Biophys Grad Program, BR-15054000 Sao Jose do Rio Preto, SP, Brazil | |
dc.description.affiliationUnesp | UNESP, IBILCE, Dept Phys, BR-15054000 Sao Jose do Rio Preto, SP, Brazil | |
dc.format.extent | 724-730 | |
dc.identifier | http://eurekaselect.com/83070/article | |
dc.identifier.citation | Protein and Peptide Letters. Sharjah: Bentham Science Publ Ltd, v. 15, n. 7, p. 724-730, 2008. | |
dc.identifier.issn | 0929-8665 | |
dc.identifier.lattes | 9162508978945887 | |
dc.identifier.lattes | 6955258588672130 | |
dc.identifier.orcid | 0000-0003-2460-1145 | |
dc.identifier.uri | http://hdl.handle.net/11449/22025 | |
dc.identifier.wos | WOS:000259509600012 | |
dc.language.iso | eng | |
dc.publisher | Bentham Science Publ Ltd | |
dc.relation.ispartof | Protein and Peptide Letters | |
dc.relation.ispartofjcr | 1.039 | |
dc.relation.ispartofsjr | 0,429 | |
dc.rights.accessRights | Acesso restrito | |
dc.source | Web of Science | |
dc.subject | Medicinal plant | en |
dc.subject | latex | en |
dc.subject | Euphorbia milii | en |
dc.subject | serine protease | en |
dc.subject | Purification | en |
dc.subject | Characterization | en |
dc.title | Purification, biochemical and functional characterization of miliin, a new thiol-dependent serine protease isolated from the latex of Euphorbia milii | en |
dc.type | Artigo | |
dcterms.license | http://www.benthamscience.com/permission.php | |
dcterms.rightsHolder | Bentham Science Publ Ltd | |
dspace.entity.type | Publication | |
unesp.author.lattes | 6955258588672130 | |
unesp.author.lattes | 9162508978945887[6] | |
unesp.author.orcid | 0000-0003-2460-1145[6] | |
unesp.campus | Universidade Estadual Paulista (UNESP), Instituto de Biociências, Letras e Ciências Exatas, São José do Rio Preto | pt |
unesp.department | Física - IBILCE | pt |
unesp.department | Química e Ciências Ambientais - IBILCE | pt |
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