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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/22025
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dc.contributor.authorMoro, L. P.-
dc.contributor.authorMurakami, M. T.-
dc.contributor.authorCabral, Hamilton-
dc.contributor.authorVidotto, A.-
dc.contributor.authorTajara, E. H.-
dc.contributor.authorArni, R. K.-
dc.contributor.authorJuliano, L.-
dc.contributor.authorBonilla-Rodriguez, Gustavo Orlando-
dc.date.accessioned2014-05-20T14:02:29Z-
dc.date.accessioned2016-10-25T17:09:08Z-
dc.date.available2014-05-20T14:02:29Z-
dc.date.available2016-10-25T17:09:08Z-
dc.date.issued2008-07-01-
dc.identifierhttp://eurekaselect.com/83070/article-
dc.identifier.citationProtein and Peptide Letters. Sharjah: Bentham Science Publ Ltd, v. 15, n. 7, p. 724-730, 2008.-
dc.identifier.issn0929-8665-
dc.identifier.urihttp://hdl.handle.net/11449/22025-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/22025-
dc.description.abstractMiliin, 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.format.extent724-730-
dc.language.isoeng-
dc.publisherBentham Science Publ Ltd-
dc.sourceWeb of Science-
dc.subjectMedicinal planten
dc.subjectlatexen
dc.subjectEuphorbia miliien
dc.subjectserine proteaseen
dc.subjectPurificationen
dc.subjectCharacterizationen
dc.titlePurification, biochemical and functional characterization of miliin, a new thiol-dependent serine protease isolated from the latex of Euphorbia miliien
dc.typeoutro-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.contributor.institutionCtr Struct Mol Biol-
dc.contributor.institutionUniversidade de São Paulo (USP)-
dc.contributor.institutionFaculdade de Medicina de São José do Rio Preto (FAMERP)-
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)-
dc.description.affiliationUNESP, IBILCE, DQCA, Dept Chem & Environm Sci, BR-15054000 Sao Jose do Rio Preto, SP, Brazil-
dc.description.affiliationUNESP, IBILCE, Mol Biophys Grad Program, BR-15054000 Sao Jose do Rio Preto, SP, Brazil-
dc.description.affiliationCtr Struct Mol Biol, Campinas, SP, Brazil-
dc.description.affiliationUniv São Paulo, Fac Pharm, BR-14049 Ribeirao Preto, SP, Brazil-
dc.description.affiliationFAMERP, Dept Mol Biol, Sao Jose do Rio Preto, SP, Brazil-
dc.description.affiliationUNESP, IBILCE, Dept Phys, BR-15054000 Sao Jose do Rio Preto, SP, Brazil-
dc.description.affiliationUniv Fed São Paulo, Dept Biophys, São Paulo, Brazil-
dc.description.affiliationUnespUNESP, IBILCE, DQCA, Dept Chem & Environm Sci, BR-15054000 Sao Jose do Rio Preto, SP, Brazil-
dc.description.affiliationUnespUNESP, IBILCE, Mol Biophys Grad Program, BR-15054000 Sao Jose do Rio Preto, SP, Brazil-
dc.description.affiliationUnespUNESP, IBILCE, Dept Phys, BR-15054000 Sao Jose do Rio Preto, SP, Brazil-
dc.identifier.wosWOS:000259509600012-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofProtein and Peptide Letters-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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