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dc.contributor.author Krause, K.
dc.contributor.author Brophy, Peter M.
dc.contributor.author Walter, R. D.
dc.contributor.author Boettcher, K.
dc.contributor.author Liebau, E.
dc.contributor.author Sommer, A.
dc.contributor.author Fischer, P.
dc.date.accessioned 2009-11-10T08:45:43Z
dc.date.available 2009-11-10T08:45:43Z
dc.date.issued 2001
dc.identifier.citation Krause , K , Brophy , P M , Walter , R D , Boettcher , K , Liebau , E , Sommer , A & Fischer , P 2001 , ' A stress-responsive glyoxalase I from the parasitic nematode Onchocerca volvulus ' Biochemical Journal , vol 353 , pp. 445-452 . en
dc.identifier.issn 1470-8728
dc.identifier.other PURE: 127686
dc.identifier.other dspace: 2160/3462
dc.identifier.uri http://hdl.handle.net/2160/3462
dc.identifier.uri http://www.biochemj.org/bj/353/0445/bj3530445.htm en
dc.description Sommer, A., Fischer, P., Krause, K., Boettcher, K., Brophy, P. M., Walter, R. D., Liebau, E. (2001). A stress-responsive glyoxalase I from the parasitic nematode Onchocerca volvulus.  Biochemical Journal, 353, 445-452. Sponsorship: Deutsche Forschungsgemeinschaft (DFG project Li 791/1-4). en
dc.description.abstract Glyoxal, methylglyoxal and other physiological a-oxoaldehydes are formed by the lipid peroxidation, glycation and degradation of glycolytic intermediates. They are detoxified enzymically by the glyoxalase system. To investigate the physiological function of glyoxalase I in parasitic organisms, the cDNA for glyoxalase I from the filarial nematode Onchocerca volvulus (designated Ov-GloI) has been cloned and characterized. The isolated cDNA contains an open reading frame of 579bp encoding a protein with a calculated molecular mass of 21930Da. Owing to the high degree of sequence identity (60%) with human glyoxalase I, for which the X-ray structure is available, it has been possible to build a three-dimensional model of Ov-GloI. The modelled core of Ov-GloI is conserved compared with the human glyoxalase I; however, there are critical differences in the residues lining the hydrophobic substrate-binding pocket of Ov-GloI. A 22kDa protein was obtained by heterologous expression in Escherichia coli. A homogeneous enzyme preparation was obtained by affinity purification and functional characterization of the recombinant enzyme included the determination of kinetic constants for methylglyoxal and phenylglyoxal as well as inhibition studies. Gel filtration demonstrated a dimeric structure. To assess the role of Ov-GloI as a potential vaccine candidate or serodiagnostic tool, the serological reactivity of the recombinant Ov-GloI was analysed with sera from microfilaria carriers and specific IgG1 antibodies were detected. The effects of oxidative insult, namely plumbagin and xanthine/xanthine oxidase, on the gene transcript level of Ov-GloI were investigated. By using a semi-quantitative PCR ELISA it was shown that Ov-GloI is expressed at elevated levels under conditions of oxidative stress. en
dc.format.extent 8 en
dc.language.iso eng
dc.relation.ispartof Biochemical Journal en
dc.subject glutathione en
dc.subject oxidative stress en
dc.subject parasite en
dc.title A stress-responsive glyoxalase I from the parasitic nematode Onchocerca volvulus en
dc.type Text en
dc.type.publicationtype Article (Journal) en
dc.contributor.institution Institute of Biological, Environmental and Rural Sciences en
dc.description.status Peer reviewed en


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