Purification, biochemical and functional characterization of miliin, a new thiol-dependent serine protease isolated from the latex of Euphorbia milii

dc.contributorUniversidade Estadual Paulista (Unesp)
dc.contributorCtr Struct Mol Biol
dc.contributorUniversidade de São Paulo (USP)
dc.contributorFaculdade de Medicina de São José do Rio Preto (FAMERP)
dc.contributorUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2014-05-20T14:02:29Z
dc.date.accessioned2022-10-05T14:50:38Z
dc.date.available2014-05-20T14:02:29Z
dc.date.available2022-10-05T14:50:38Z
dc.date.created2014-05-20T14:02:29Z
dc.date.issued2008-07-01
dc.identifierProtein and Peptide Letters. Sharjah: Bentham Science Publ Ltd, v. 15, n. 7, p. 724-730, 2008.
dc.identifier0929-8665
dc.identifierhttp://hdl.handle.net/11449/22025
dc.identifierWOS:000259509600012
dc.identifier9162508978945887
dc.identifier6955258588672130
dc.identifier0000-0003-2460-1145
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/3895710
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.
dc.languageeng
dc.publisherBentham Science Publ Ltd
dc.relationProtein and Peptide Letters
dc.relation1.039
dc.relation0,429
dc.rightsAcesso restrito
dc.sourceWeb of Science
dc.subjectMedicinal plant
dc.subjectlatex
dc.subjectEuphorbia milii
dc.subjectserine protease
dc.subjectPurification
dc.subjectCharacterization
dc.titlePurification, biochemical and functional characterization of miliin, a new thiol-dependent serine protease isolated from the latex of Euphorbia milii
dc.typeArtigo


Este ítem pertenece a la siguiente institución