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

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

Autor Cabral, H. Google Scholar
Leopoldino, A. M. Google Scholar
Tajara, E. H. Google Scholar
Greene, L. J. Google Scholar
Faca, V. M. Google Scholar
Mateus, R. P. Google Scholar
Ceron, C. R. Google Scholar
Judice, WAD Google Scholar
Juliano, Luiz Autor UNIFESP Google Scholar
Bonilla-Rodriguez, G. O. Google Scholar
Instituição UNESP
Universidade de São Paulo (USP)
Universidade Federal de São Paulo (UNIFESP)
Resumo The 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%).
Palavra-chave peptidase
plant peptidase
papain
bromelain
cysteine-protease
protease
Idioma Inglês
Data de publicação 2006-01-01
Publicado em Protein and Peptide Letters. Sharjah: Bentham Science Publ Ltd, v. 13, n. 1, p. 83-89, 2006.
ISSN 0929-8665 (Sherpa/Romeo, fator de impacto)
Publicador Bentham Science Publ Ltd
Extensão 83-89
Fonte http://dx.doi.org/10.2174/092986606774502072
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000233942400014
Endereço permanente http://repositorio.unifesp.br/handle/11600/28685

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