A recombinant glutathione S-transferase (GST) (EC 2.5.1.18) from the parasitic nematode Ascaris suum(AsGST1) displays specific activity with a variety of model substrates and secondary products of lipid peroxidation. The AsGST1 interacts with a range of model inhibitors, haematin-related compounds, bile acids and anthelminthics. The reported variations in biochemical activity correlate with structural differences observed by homology modelling. Here, differences in the topography of the proposed substrate binding site between the AsGST1 and the host GSTs were identified. A rabbit polyclonal antiserum was raised against the glutathione-binding proteins ofA. suum and specific antibodies against AsGST1 were affinity-purified using the recombinant protein. These antibodies were used to localize the AsGST1 in adult worms by immunohistochemical staining. The strongest immunostaining for AsGST1 was localized in the intestine in all worms examined. This suggests that the enzyme may be responsible for the metabolism of materials that are incorporated from the environment, as well as for molecules that are excreted or secreted from the parasite to the environment. It also demonstrates the accessibility of the enzyme to an inhibitor or blocking antibody. In addition, the structure and sequence of the gene encoding AsGST1 have been determined. Southern-blot analyses of the AsGST1 gene suggests that it is a single-copy gene. The nucleotide sequence analysis revealed that the gene is composed of four exons and three introns, and potential regulatory elements were identified in the 5′ flanking sequence.
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June 1997
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Research Article|
June 01 1997
Structural and functional analysis of a glutathione S-transferase from Ascaris suum
Eva LIEBAU;
Eva LIEBAU
§
*Department of Biochemical Parasitology, Bernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Str. 74, D-20359 Hamburg
§To whom correspondence should be addressed.
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Volker H. O. ECKELT;
Volker H. O. ECKELT
*Department of Biochemical Parasitology, Bernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Str. 74, D-20359 Hamburg
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Gabriele WILDENBURG;
Gabriele WILDENBURG
†Department of Helminthology, Bernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Str. 74, D-20359 Hamburg, Germany
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Paul TEESDALE-SPITTLE;
Paul TEESDALE-SPITTLE
‡School of Applied Sciences, De Montfort University, Leicester LE1 9BH, U.K.
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Peter M. BROPHY;
Peter M. BROPHY
‡School of Applied Sciences, De Montfort University, Leicester LE1 9BH, U.K.
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Rolf D. WALTER;
Rolf D. WALTER
*Department of Biochemical Parasitology, Bernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Str. 74, D-20359 Hamburg
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Kimberly HENKLE-DÜHRSEN
Kimberly HENKLE-DÜHRSEN
*Department of Biochemical Parasitology, Bernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Str. 74, D-20359 Hamburg
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Publisher: Portland Press Ltd
Received:
October 15 1996
Revision Received:
January 31 1997
Accepted:
February 11 1997
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London © 1997
1997
Biochem J (1997) 324 (2): 659–666.
Article history
Received:
October 15 1996
Revision Received:
January 31 1997
Accepted:
February 11 1997
Citation
Eva LIEBAU, Volker H. O. ECKELT, Gabriele WILDENBURG, Paul TEESDALE-SPITTLE, Peter M. BROPHY, Rolf D. WALTER, Kimberly HENKLE-DÜHRSEN; Structural and functional analysis of a glutathione S-transferase from Ascaris suum. Biochem J 1 June 1997; 324 (2): 659–666. doi: https://doi.org/10.1042/bj3240659
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