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Type: Artigo de periódico
Title: Cloning, expression, and purification of the virulence-associated protein D from Xylella fastidiosa
Author: Catani, CF
Azzoni, AR
Paula, DP
Tada, SFS
Rosselli, LK
de Souza, AP
Yano, T
Abstract: in this study, an efficient expression system, based on the pET32Xa/LIC vector, for producing a Xylella fastidiosa virulence-associated protein D, found to have a strong similarity to Riemerella anatipestifer and Actinobacillus actinomycetencomitans VapD protein, is presented. The protein has a molecular mass of 17.637 Da and a calculated pI of 5.49. The selected XFa0052 gene was cloned in the pET32Xa/LIC vector and the plasmid was transformed into Escherichia coli BL21 (DE3) strain at 37degreesC. with an induction time of 2 h and 1 mM IPTG concentration. The protein present in the soluble fraction was purified by immobilized metal affinity chromatography (IMAC), and had its identity determined by mass spectrometry (MALDI-TOF) and N-terminal sequencing. The purified protein was found as a single band on SDS-PAGE and its correct folding was verified by circular dichroism spectroscopy. (C) 2004 Elsevier Inc. All rights reserved.
Subject: VapD protein
expression and purification
Xylella fastidiosa
Country: EUA
Editor: Academic Press Inc Elsevier Science
Citation: Protein Expression And Purification. Academic Press Inc Elsevier Science, v. 37, n. 2, n. 320, n. 326, 2004.
Rights: fechado
Identifier DOI: 10.1016/j.pep.2004.07.002
Date Issue: 2004
Appears in Collections:Unicamp - Artigos e Outros Documentos

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