Preliminary functional characterization, cloning and primary sequence of Fastuosain, a cysteine peptidase isolated from fruits of Bromelia fastuosa

dc.contributorUniversidade Estadual Paulista (Unesp)
dc.contributorUniversidade de São Paulo (USP)
dc.contributorUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2014-05-20T14:03:01Z
dc.date.available2014-05-20T14:03:01Z
dc.date.created2014-05-20T14:03:01Z
dc.date.issued2006-01-01
dc.identifierProtein and Peptide Letters. Sharjah: Bentham Science Publ Ltd, v. 13, n. 1, p. 83-89, 2006.
dc.identifier0929-8665
dc.identifierhttp://hdl.handle.net/11449/22208
dc.identifier10.2174/092986606774502072
dc.identifierWOS:000233942400014
dc.identifier2307201085881971
dc.description.abstractThe present work reports the characterization of Fastuosain, a novel cysteine protease of 25kDa, purified from the unripe fruits of Bromelia fastuosa, a wild South American Bromeliaceae. Proteolytic activity, measured using casein and synthetic substrates, was dependent on the presence of thiol reagents, having maximum activity at pH 7.0. The present work reports cDNA cloning of Fastuosain; cDNA was amplified by PCR using specific primers. The product was 1096pb long. Mature fastuosain has 217 residues, and with the proregion has a total length of 324 residues. Its primary sequence showed high homology with ananain(74%), stem bromelain (66%) and papain (44%).
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.subjectPeptidase
dc.subjectplant peptidase
dc.subjectpapain
dc.subjectbromelain
dc.subjectcysteine-protease
dc.subjectprotease
dc.titlePreliminary functional characterization, cloning and primary sequence of Fastuosain, a cysteine peptidase isolated from fruits of Bromelia fastuosa
dc.typeArtículos de revistas


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