dc.creatorAbreu Payrol, Juan
dc.creatorObregón, Walter David
dc.creatorTrejo, Sebastián Alejandro
dc.creatorCaffini, Néstor Oscar
dc.date2008-02
dc.date2022-03-28T14:57:40Z
dc.date.accessioned2023-07-15T04:43:43Z
dc.date.available2023-07-15T04:43:43Z
dc.identifierhttp://sedici.unlp.edu.ar/handle/10915/133375
dc.identifierissn:1572-3887
dc.identifierissn:1573-4943
dc.identifierissn:0277-8033
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/7470658
dc.description<i>Bromelia pinguin</i> L. is a plant broadly distributed in Central America and Caribbean islands. The fruits have been used in traditional medicine as anthelmintic, probably owed to the presence of a mixture of cysteine endopeptidases, initially termed pinguinain. This work deals with the purification and characterization of the four main components of that mixture, two of them showing acid pI and the other two alkaline pI. Molecular masses (SDS-PAGE and MALDI-TOF), N-terminal sequence and the reactivity and kinetic parameters versus synthetic substrates (p-nitrophenyl-N-α-CBZ-amino acid esters, PFLNA, Z-Arg-Arg-p-NA, and Z-Phe-Arg-p-NA) of the studied peptidases are given, as well as the N-terminal sequences of the enzymes and the homology degree with other plant endopeptidases.
dc.descriptionFacultad de Ciencias Exactas
dc.descriptionCentro de Investigación de Proteínas Vegetales
dc.formatapplication/pdf
dc.format88-96
dc.languageen
dc.rightshttp://creativecommons.org/licenses/by/4.0/
dc.rightsCreative Commons Attribution 4.0 International (CC BY 4.0)
dc.subjectCiencias Exactas
dc.subjectBiología
dc.subjectBromelia pinguin L.
dc.subjectBromeliaceae
dc.subjectPlant cysteine endopeptidases
dc.subjectPinguinain
dc.titlePurification and Characterization of Four New Cysteine Endopeptidases From Fruits of <i>Bromelia pinguin</i> L. Grown in Cuba
dc.typeArticulo
dc.typeArticulo


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