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.contributorLaboratory
dc.contributorUniversidade de São Paulo (USP)
dc.contributorFAMERP
dc.contributorUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2022-04-28T20:43:08Z
dc.date.accessioned2022-12-20T01:59:23Z
dc.date.available2022-04-28T20:43:08Z
dc.date.available2022-12-20T01:59:23Z
dc.date.created2022-04-28T20:43:08Z
dc.date.issued2008-07-01
dc.identifierProtein and Peptide Letters, v. 15, n. 7, p. 724-730, 2008.
dc.identifier0929-8665
dc.identifierhttp://hdl.handle.net/11449/225247
dc.identifier10.2174/092986608785133744
dc.identifier2-s2.0-49449115536
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/5405377
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°C in the pH range of and 7.5-11.0. Activity tests indicate that milliin is a thiol-dependent serine protease. © 2008 Bentham Science Publishers Ltd.
dc.languageeng
dc.relationProtein and Peptide Letters
dc.sourceScopus
dc.subjectCharacterization
dc.subjectEuphorbia milii
dc.subjectLatex
dc.subjectMedicinal plant
dc.subjectPurification
dc.subjectSerine protease
dc.titlePurification, biochemical and functional characterization of miliin, a new thiol-dependent serine protease isolated from the latex of Euphorbia milii
dc.typeArtículos de revistas


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