Purification of cytosolic glutathione transferases from Schistocephalus solidus (plerocercoid): interaction with anthelmintics and products of lipid peroxidation
Glutathione (GSH) transferase isoenzymes have been partially resolved from the cytosol of Schistocephalus solidus (plerocercoid) by GSH affinity chromatography and chromatofocusing at pH 7-5. The presence of isomeric forms was also suggested by analytical isoelectric focusing and high-performance li...
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| Veröffentlicht in: | Molecular and biochemical parasitology 1989-09, Vol.36 (2), p.187-196 |
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| creator | Brophy, Peter M. Papadopoulos, Athanasios Touraki, Maria Coles, Brian Körting, Wolfgang Barrett, John |
| description | Glutathione (GSH) transferase isoenzymes have been partially resolved from the cytosol of
Schistocephalus solidus (plerocercoid) by GSH affinity chromatography and chromatofocusing at pH 7-5. The presence of isomeric forms was also suggested by analytical isoelectric focusing and high-performance liquid chromatography (HPLC). Gel filtration and sodium dodecyl sulphate-polyacrylamide gel electrophoresis indicated that GSH transferase forms were dimers with a subunit size of approximately 24 kDa. The major GSH transferase form in
S. solidus (plerocercoid) showed greater biochemical relationship to the Mu family of mammalian GSH transferase compared to the mammalian Alpha or Pi families. The major subunit purified by GSH affinity chromatography and reversed-phase HPLC also showed high N-terminal homology with the Mu family. A minor GSH transferase form appeared more biochemically related to the Alpha family with respect to substrate specificity and inhibitor sensitivity. The major GSH transferase was inhibited by haematin-related compounds, bile acids and a number of anthelmintics including members of the benzimidazole and phenol-based class of compounds. The major GSH transferase had conjugating activity with members of the
trans,
trans-2,4-alkadienal and
trans-2-alkenal series, secondary products of lipid peroxidation. |
| doi_str_mv | 10.1016/0166-6851(89)90191-6 |
| format | Article |
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Schistocephalus solidus (plerocercoid) by GSH affinity chromatography and chromatofocusing at pH 7-5. The presence of isomeric forms was also suggested by analytical isoelectric focusing and high-performance liquid chromatography (HPLC). Gel filtration and sodium dodecyl sulphate-polyacrylamide gel electrophoresis indicated that GSH transferase forms were dimers with a subunit size of approximately 24 kDa. The major GSH transferase form in
S. solidus (plerocercoid) showed greater biochemical relationship to the Mu family of mammalian GSH transferase compared to the mammalian Alpha or Pi families. The major subunit purified by GSH affinity chromatography and reversed-phase HPLC also showed high N-terminal homology with the Mu family. A minor GSH transferase form appeared more biochemically related to the Alpha family with respect to substrate specificity and inhibitor sensitivity. The major GSH transferase was inhibited by haematin-related compounds, bile acids and a number of anthelmintics including members of the benzimidazole and phenol-based class of compounds. The major GSH transferase had conjugating activity with members of the
trans,
trans-2,4-alkadienal and
trans-2-alkenal series, secondary products of lipid peroxidation.</description><identifier>ISSN: 0166-6851</identifier><identifier>EISSN: 1872-9428</identifier><identifier>DOI: 10.1016/0166-6851(89)90191-6</identifier><identifier>PMID: 2770789</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>aculeatus aculeatus ; Amino Acid Sequence ; Animals ; anthelmintic agents ; Anthelmintic, Lipid peroxidation ; Anthelmintics - pharmacology ; Cestoda - enzymology ; Chromatography, Affinity ; Chromatography, Gel ; Cytosol - enzymology ; Electrophoresis, Polyacrylamide Gel ; Gasterosteiformes ; glutathione ; Glutathione transferase ; Glutathione Transferase - antagonists & inhibitors ; Glutathione Transferase - isolation & purification ; Glutathione Transferase - metabolism ; Isoenzymes - metabolism ; Lipid Peroxidation ; Molecular Sequence Data ; Rats ; Schistocephalus ; Schistocephalus solidus ; Schistocephalus solidus (plerocercoid) ; Substrate Specificity ; transferases</subject><ispartof>Molecular and biochemical parasitology, 1989-09, Vol.36 (2), p.187-196</ispartof><rights>1989</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c412t-894103a0d839b846e98fc52f56cd196550db6f60e182eacd777cdbf04149d7e83</citedby><cites>FETCH-LOGICAL-c412t-894103a0d839b846e98fc52f56cd196550db6f60e182eacd777cdbf04149d7e83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0166-6851(89)90191-6$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2770789$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Brophy, Peter M.</creatorcontrib><creatorcontrib>Papadopoulos, Athanasios</creatorcontrib><creatorcontrib>Touraki, Maria</creatorcontrib><creatorcontrib>Coles, Brian</creatorcontrib><creatorcontrib>Körting, Wolfgang</creatorcontrib><creatorcontrib>Barrett, John</creatorcontrib><title>Purification of cytosolic glutathione transferases from Schistocephalus solidus (plerocercoid): interaction with anthelmintics and products of lipid peroxidation</title><title>Molecular and biochemical parasitology</title><addtitle>Mol Biochem Parasitol</addtitle><description>Glutathione (GSH) transferase isoenzymes have been partially resolved from the cytosol of
Schistocephalus solidus (plerocercoid) by GSH affinity chromatography and chromatofocusing at pH 7-5. The presence of isomeric forms was also suggested by analytical isoelectric focusing and high-performance liquid chromatography (HPLC). Gel filtration and sodium dodecyl sulphate-polyacrylamide gel electrophoresis indicated that GSH transferase forms were dimers with a subunit size of approximately 24 kDa. The major GSH transferase form in
S. solidus (plerocercoid) showed greater biochemical relationship to the Mu family of mammalian GSH transferase compared to the mammalian Alpha or Pi families. The major subunit purified by GSH affinity chromatography and reversed-phase HPLC also showed high N-terminal homology with the Mu family. A minor GSH transferase form appeared more biochemically related to the Alpha family with respect to substrate specificity and inhibitor sensitivity. The major GSH transferase was inhibited by haematin-related compounds, bile acids and a number of anthelmintics including members of the benzimidazole and phenol-based class of compounds. The major GSH transferase had conjugating activity with members of the
trans,
trans-2,4-alkadienal and
trans-2-alkenal series, secondary products of lipid peroxidation.</description><subject>aculeatus aculeatus</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>anthelmintic agents</subject><subject>Anthelmintic, Lipid peroxidation</subject><subject>Anthelmintics - pharmacology</subject><subject>Cestoda - enzymology</subject><subject>Chromatography, Affinity</subject><subject>Chromatography, Gel</subject><subject>Cytosol - enzymology</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Gasterosteiformes</subject><subject>glutathione</subject><subject>Glutathione transferase</subject><subject>Glutathione Transferase - antagonists & inhibitors</subject><subject>Glutathione Transferase - isolation & purification</subject><subject>Glutathione Transferase - metabolism</subject><subject>Isoenzymes - metabolism</subject><subject>Lipid Peroxidation</subject><subject>Molecular Sequence Data</subject><subject>Rats</subject><subject>Schistocephalus</subject><subject>Schistocephalus solidus</subject><subject>Schistocephalus solidus (plerocercoid)</subject><subject>Substrate Specificity</subject><subject>transferases</subject><issn>0166-6851</issn><issn>1872-9428</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUV1rFDEUHUSpa_UfKOZJ2ofRZCaffRCk-AUFhdrnkE1uOpGZyZpk1P4c_6mZ3aWPGgiXnHvOyU1O0zwn-DXBhL-pm7dcMnIm1bnCRJGWP2g2RIquVbSTD5vNPeVx8yTn7xhjJjg_aU46IbCQatP8-bqk4IM1JcQZRY_sXYk5jsGi23EppgwVB1SSmbOHZDJk5FOc0LUdQi7Rwm4w45LRqnG1nu1GSBVONgZ3foHCXKrM7u1_hTIgM5cBxqniweZ6cmiXoltsyev1Y9iFilSL38Hth3raPPJmzPDsWE-bmw_vv11-aq--fPx8-e6qtZR0pZWKEtwb7GSvtpJyUNJb1nnGrSOKM4bdlnuOgcgOjHVCCOu2HlNClRMg-9Pm1cG3jvNjgVz0FLKFcTQzxCVroYiifV3_IxJGGWN9V4n0QLQp5pzA610Kk0l3mmC9RqjXfPSaj5ZK7yPUvMpeHP2X7QTuXnTMrPZfHvreRG1uU8j65rrDpMcdF4LK9SlvDwyo__UzQNLZBpgtuJDAFu1i-PcIfwEoDrkt</recordid><startdate>19890901</startdate><enddate>19890901</enddate><creator>Brophy, Peter M.</creator><creator>Papadopoulos, Athanasios</creator><creator>Touraki, Maria</creator><creator>Coles, Brian</creator><creator>Körting, Wolfgang</creator><creator>Barrett, John</creator><general>Elsevier B.V</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19890901</creationdate><title>Purification of cytosolic glutathione transferases from Schistocephalus solidus (plerocercoid): interaction with anthelmintics and products of lipid peroxidation</title><author>Brophy, Peter M. ; Papadopoulos, Athanasios ; Touraki, Maria ; Coles, Brian ; Körting, Wolfgang ; Barrett, John</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c412t-894103a0d839b846e98fc52f56cd196550db6f60e182eacd777cdbf04149d7e83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>aculeatus aculeatus</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>anthelmintic agents</topic><topic>Anthelmintic, Lipid peroxidation</topic><topic>Anthelmintics - pharmacology</topic><topic>Cestoda - enzymology</topic><topic>Chromatography, Affinity</topic><topic>Chromatography, Gel</topic><topic>Cytosol - enzymology</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Gasterosteiformes</topic><topic>glutathione</topic><topic>Glutathione transferase</topic><topic>Glutathione Transferase - antagonists & inhibitors</topic><topic>Glutathione Transferase - isolation & purification</topic><topic>Glutathione Transferase - metabolism</topic><topic>Isoenzymes - metabolism</topic><topic>Lipid Peroxidation</topic><topic>Molecular Sequence Data</topic><topic>Rats</topic><topic>Schistocephalus</topic><topic>Schistocephalus solidus</topic><topic>Schistocephalus solidus (plerocercoid)</topic><topic>Substrate Specificity</topic><topic>transferases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Brophy, Peter M.</creatorcontrib><creatorcontrib>Papadopoulos, Athanasios</creatorcontrib><creatorcontrib>Touraki, Maria</creatorcontrib><creatorcontrib>Coles, Brian</creatorcontrib><creatorcontrib>Körting, Wolfgang</creatorcontrib><creatorcontrib>Barrett, John</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular and biochemical parasitology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Brophy, Peter M.</au><au>Papadopoulos, Athanasios</au><au>Touraki, Maria</au><au>Coles, Brian</au><au>Körting, Wolfgang</au><au>Barrett, John</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification of cytosolic glutathione transferases from Schistocephalus solidus (plerocercoid): interaction with anthelmintics and products of lipid peroxidation</atitle><jtitle>Molecular and biochemical parasitology</jtitle><addtitle>Mol Biochem Parasitol</addtitle><date>1989-09-01</date><risdate>1989</risdate><volume>36</volume><issue>2</issue><spage>187</spage><epage>196</epage><pages>187-196</pages><issn>0166-6851</issn><eissn>1872-9428</eissn><abstract>Glutathione (GSH) transferase isoenzymes have been partially resolved from the cytosol of
Schistocephalus solidus (plerocercoid) by GSH affinity chromatography and chromatofocusing at pH 7-5. The presence of isomeric forms was also suggested by analytical isoelectric focusing and high-performance liquid chromatography (HPLC). Gel filtration and sodium dodecyl sulphate-polyacrylamide gel electrophoresis indicated that GSH transferase forms were dimers with a subunit size of approximately 24 kDa. The major GSH transferase form in
S. solidus (plerocercoid) showed greater biochemical relationship to the Mu family of mammalian GSH transferase compared to the mammalian Alpha or Pi families. The major subunit purified by GSH affinity chromatography and reversed-phase HPLC also showed high N-terminal homology with the Mu family. A minor GSH transferase form appeared more biochemically related to the Alpha family with respect to substrate specificity and inhibitor sensitivity. The major GSH transferase was inhibited by haematin-related compounds, bile acids and a number of anthelmintics including members of the benzimidazole and phenol-based class of compounds. The major GSH transferase had conjugating activity with members of the
trans,
trans-2,4-alkadienal and
trans-2-alkenal series, secondary products of lipid peroxidation.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>2770789</pmid><doi>10.1016/0166-6851(89)90191-6</doi><tpages>10</tpages></addata></record> |
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| ispartof | Molecular and biochemical parasitology, 1989-09, Vol.36 (2), p.187-196 |
| issn | 0166-6851 1872-9428 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_79194333 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | aculeatus aculeatus Amino Acid Sequence Animals anthelmintic agents Anthelmintic, Lipid peroxidation Anthelmintics - pharmacology Cestoda - enzymology Chromatography, Affinity Chromatography, Gel Cytosol - enzymology Electrophoresis, Polyacrylamide Gel Gasterosteiformes glutathione Glutathione transferase Glutathione Transferase - antagonists & inhibitors Glutathione Transferase - isolation & purification Glutathione Transferase - metabolism Isoenzymes - metabolism Lipid Peroxidation Molecular Sequence Data Rats Schistocephalus Schistocephalus solidus Schistocephalus solidus (plerocercoid) Substrate Specificity transferases |
| title | Purification of cytosolic glutathione transferases from Schistocephalus solidus (plerocercoid): interaction with anthelmintics and products of lipid peroxidation |
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