Show simple item record

dc.contributor.author Barrett, John
dc.contributor.author Jefferies, James R.
dc.contributor.author Campbell, Alison M.
dc.contributor.author van Rossum, Arjan J.
dc.contributor.author Brophy, Peter M.
dc.date.accessioned 2009-10-28T11:38:59Z
dc.date.available 2009-10-28T11:38:59Z
dc.date.issued 2001-09-18
dc.identifier.citation Barrett , J , Jefferies , J R , Campbell , A M , van Rossum , A J & Brophy , P M 2001 , ' Proteomic analysis of Fasciola hepatica excretory-secretory products ' Proteomics , vol 1 , no. 9 , pp. 1128-1132 . , 10.1002/1615-9861(200109)1:9<1128::AID-PROT1128>3.0.CO;2-0 en
dc.identifier.issn 1615-9861
dc.identifier.other PURE: 125757
dc.identifier.other dspace: 2160/3341
dc.identifier.uri http://hdl.handle.net/2160/3341
dc.description Jefferies, J. R., Campbell, A. M., van Rossum, A. J., Barrett, J., Brophy, P. M. (2001). Proteomic analysis of Fasciola hepatica excretory-secretory products.   Proteomics, 1, (9), 1128-1132. Sponsorship: BBSRC en
dc.description.abstract This paper describes a global investigation of the components of Fasciola hepatica excretory-secretory (ES) products by a proteomic approach. Despite the absence of a F. hepatica genome sequencing project we have shown that it was possible to identify 29 of the 60 prominent proteins found using two-dimensional gel electrophoresis. As well as cathepsin L proteases, a number of enzymes implicated in parasite protection from the host immune system were also found to be present in relatively large abundance. These included superoxide dismutase, thioredoxin peroxidase, glutathione S-transferases and fatty acid binding proteins, all of which may play a part in the detoxification of reactive oxygen intermediates. Interestingly, ovine superoxide dismutase was the only protein from the host identified on the gel. We suggest that the relative abundance and protective nature of the components of the ES products of this organism play an important role in its survival within the host. The precise identification, to individual NCBI database entries, of a number of glutathione S-transferases and cathepsin Ls from F. hepatica, by peptide mass fingerprinting, was hampered by multidatabase submissions of the two protein superfamilies from this organism. en
dc.format.extent 5 en
dc.language.iso eng
dc.relation.ispartof Proteomics en
dc.subject Excretory-secretory produce en
dc.subject Fasciola hepatica en
dc.subject Peptide mass fingerprinting en
dc.subject Glutathione-S-transferase en
dc.subject Fatty acid binding protein en
dc.title Proteomic analysis of Fasciola hepatica excretory-secretory products en
dc.type Text en
dc.type.publicationtype Article (Journal) en
dc.identifier.doi http://dx.doi.org/10.1002/1615-9861(200109)1:9<1128::AID-PROT1128>3.0.CO;2-0
dc.contributor.institution Institute of Biological, Environmental and Rural Sciences en
dc.description.status Peer reviewed en


Files in this item

Files Size Format View

There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record

Search Cadair


Advanced Search

Browse

Statistics