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dc.contributor.author Chemale, Gustavo
dc.contributor.author Barrett, John
dc.contributor.author Zaha, A.
dc.contributor.author Ferreira, Henrique B.
dc.contributor.author Brophy, Peter M.
dc.date.accessioned 2009-11-26T17:03:26Z
dc.date.available 2009-11-26T17:03:26Z
dc.date.issued 2005-03-14
dc.identifier.citation Chemale , G , Barrett , J , Zaha , A , Ferreira , H B & Brophy , P M 2005 , ' Echinococcus granulosus antigen B hydrophobic ligand binding properties ' Biochimica et Biophysica Acta-Proteins and Proteomics , pp. 189-194 . , 10.1016/j.bbapap.2004.11.004 en
dc.identifier.other PURE: 140650
dc.identifier.other dspace: 2160/3697
dc.identifier.uri http://hdl.handle.net/2160/3697
dc.description Chemale, G., Ferreira, H. B., Barrett, J., Brophy, P. M., Zaha, A. (2005). Echinococcus granulosus antigen B hydrophobic ligand binding properties. Biochimica et Biophysica Acta-Proteins and Proteomics, 1747, (2), 189-194. Sponsorship: CNPq, PADCT/CNPq, FAPERGS (Brazil) / BBSRC (UK). en
dc.description.abstract Antigen B (AgB), an immunodominant component of the cestode parasite Echinococcus granulosus, presents homology to and shares apparent structural similarities with helix-rich hydrophobic ligand binding proteins (HLBPs) from other cestodes. In order to investigate the fatty acid binding properties of AgB, two of its subunit components (rAgB8/1 and rAgB8/2) were expressed in Escherichia coli and purified, and the native antigen was purified from the hydatid cyst fluid by affinity chromatography using a monoclonal antibody raised against rAgB8/1. The interaction of the purified native and recombinant proteins with the fluorescent ligands DAUDA, ANS, DACA and 16-AP was investigated. The palmitic acid derived fluorescent ligand, 16-AP, showed the greatest enhancement in fluorescence when bound to native AgB or to its recombinant subunits, and the dissociation constants for 16-AP binding were determined. Surprisingly, in contrast to HLBPs from other cestodes, interactions with other fatty acids, including palmitic acid, caused an increase in fluorescence instead of competing with 16-AP. Our results suggest that AgB might have evolved different functions in the binding of hydrophobic compounds, dependent on cestode environment. en
dc.format.extent 6 en
dc.language.iso eng
dc.relation.ispartof Biochimica et Biophysica Acta-Proteins and Proteomics en
dc.title Echinococcus granulosus antigen B hydrophobic ligand binding properties en
dc.type Text en
dc.type.publicationtype Article (Journal) en
dc.identifier.doi http://dx.doi.org/10.1016/j.bbapap.2004.11.004
dc.contributor.institution Institute of Biological, Environmental and Rural Sciences en
dc.description.status Peer reviewed en


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