Effect of acaricides on the activity of a Boophilus microplus glutathione S-transferase
In the present study, we report the effect of several acaricides on the enzyme activity of a Boophilus microplus recombinant glutathione S-transferase (rGST). GST was expressed in Escherichia coli and was purified with glutathione (GSH) affinity column chromatography. The kinetic constants were dete...
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| Veröffentlicht in: | Veterinary parasitology 2004-01, Vol.119 (2), p.237-245 |
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| creator | da Silva Vaz, Itabajara Torino Lermen, Tiago Michelon, André Sanchez Ferreira, Carlos Alexandre Joaquim de Freitas, Daniela Reis Termignoni, Carlos Masuda, Aoi |
| description | In the present study, we report the effect of several acaricides on the enzyme activity of a
Boophilus microplus recombinant glutathione S-transferase (rGST). GST was expressed in
Escherichia coli and was purified with glutathione (GSH) affinity column chromatography. The kinetic constants were determined by reacting GST with the substrates 1-chloro-2,4-dinitrobenzene (CDNB) and glutathione. We report the effect of several acaricides on the enzyme activity of rGST. Some acaricides (ethion, amitraz, chlorpyrifos, DDT, cypermethrin, diazinon, ivermectin, deltamethrin and flumethrin) inhibited rGST. Contrarily, coumaphos had an activating effect. Although the accurate mechanisms of the
B. microplus resistance to acaricides remain elusive, this work helps in understanding how acaricides can interact with GST. |
| doi_str_mv | 10.1016/j.vetpar.2003.11.004 |
| format | Article |
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Boophilus microplus recombinant glutathione S-transferase (rGST). GST was expressed in
Escherichia coli and was purified with glutathione (GSH) affinity column chromatography. The kinetic constants were determined by reacting GST with the substrates 1-chloro-2,4-dinitrobenzene (CDNB) and glutathione. We report the effect of several acaricides on the enzyme activity of rGST. Some acaricides (ethion, amitraz, chlorpyrifos, DDT, cypermethrin, diazinon, ivermectin, deltamethrin and flumethrin) inhibited rGST. Contrarily, coumaphos had an activating effect. Although the accurate mechanisms of the
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Boophilus microplus recombinant glutathione S-transferase (rGST). GST was expressed in
Escherichia coli and was purified with glutathione (GSH) affinity column chromatography. The kinetic constants were determined by reacting GST with the substrates 1-chloro-2,4-dinitrobenzene (CDNB) and glutathione. We report the effect of several acaricides on the enzyme activity of rGST. Some acaricides (ethion, amitraz, chlorpyrifos, DDT, cypermethrin, diazinon, ivermectin, deltamethrin and flumethrin) inhibited rGST. Contrarily, coumaphos had an activating effect. Although the accurate mechanisms of the
B. microplus resistance to acaricides remain elusive, this work helps in understanding how acaricides can interact with GST.</description><subject>Acaricides</subject><subject>Animals</subject><subject>Blotting, Western</subject><subject>Boophilus microplus</subject><subject>Chromatography, Affinity</subject><subject>Dinitrochlorobenzene - metabolism</subject><subject>Drug resistance</subject><subject>Escherichia coli - genetics</subject><subject>Female</subject><subject>Glutathione S-transferase</subject><subject>Glutathione Transferase - antagonists & inhibitors</subject><subject>Glutathione Transferase - metabolism</subject><subject>Insecticides - pharmacology</subject><subject>Ixodidae</subject><subject>Ixodidae - enzymology</subject><subject>Ixodidae - metabolism</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><issn>0304-4017</issn><issn>1873-2550</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEtP4zAURq0Ro6GU-QcIZcUu4Tpx7HiDBBUvCYnFzIil5To3U1dpHGynUv89Lq3EjpUt-9zHdwi5oFBQoPx6XWwxjtoXJUBVUFoAsB9kRhtR5WVdwwmZQQUsZ0DFKTkLYQ2JAC5-kVPKBOOyKWfk7b7r0MTMdZk22ltjWwyZG7K4wvQS7dbG3edvdufcuLL9FLKNNd6N-9v_foo6rqwbMPuTR6-H0KHXAc_Jz073AX8fzzn593D_d_GUv7w-Pi9uX3JTNTLmUoBuZcukaKDsUhBJBRdcL7slN61BUdfcCGQgSkkTqZdcVsxUJW9RyIpXc3J16Dt69z5hiGpjg8G-1wO6KSgqS9ZATRPIDmBaPQSPnRq93Wi_UxTUXqhaq4NQtReqKFVJVyq7PPaflhtsv4qOBhNwcwAwpdxa9CoYi4PB1vokVrXOfj_hA0KMiSQ</recordid><startdate>20040130</startdate><enddate>20040130</enddate><creator>da Silva Vaz, Itabajara</creator><creator>Torino Lermen, Tiago</creator><creator>Michelon, André</creator><creator>Sanchez Ferreira, Carlos Alexandre</creator><creator>Joaquim de Freitas, Daniela Reis</creator><creator>Termignoni, Carlos</creator><creator>Masuda, Aoi</creator><general>Elsevier B.V</general><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>7SS</scope></search><sort><creationdate>20040130</creationdate><title>Effect of acaricides on the activity of a Boophilus microplus glutathione S-transferase</title><author>da Silva Vaz, Itabajara ; 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Boophilus microplus recombinant glutathione S-transferase (rGST). GST was expressed in
Escherichia coli and was purified with glutathione (GSH) affinity column chromatography. The kinetic constants were determined by reacting GST with the substrates 1-chloro-2,4-dinitrobenzene (CDNB) and glutathione. We report the effect of several acaricides on the enzyme activity of rGST. Some acaricides (ethion, amitraz, chlorpyrifos, DDT, cypermethrin, diazinon, ivermectin, deltamethrin and flumethrin) inhibited rGST. Contrarily, coumaphos had an activating effect. Although the accurate mechanisms of the
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| identifier | ISSN: 0304-4017 |
| ispartof | Veterinary parasitology, 2004-01, Vol.119 (2), p.237-245 |
| issn | 0304-4017 1873-2550 |
| language | eng |
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| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Acaricides Animals Blotting, Western Boophilus microplus Chromatography, Affinity Dinitrochlorobenzene - metabolism Drug resistance Escherichia coli - genetics Female Glutathione S-transferase Glutathione Transferase - antagonists & inhibitors Glutathione Transferase - metabolism Insecticides - pharmacology Ixodidae Ixodidae - enzymology Ixodidae - metabolism Recombinant Proteins - genetics Recombinant Proteins - metabolism |
| title | Effect of acaricides on the activity of a Boophilus microplus glutathione S-transferase |
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