Characterization of glutathione S-transferases in juvenile white sturgeon.
Identifieur interne : 000542 ( PubMed/Corpus ); précédent : 000541; suivant : 000543Characterization of glutathione S-transferases in juvenile white sturgeon.
Auteurs : Rachel T. Donham ; Dexter Morin ; William T. Jewell ; Stephanie A. Burns ; Alyson E. Mitchell ; M W Lamé ; H J Segall ; Ronald S. TjeerdemaSource :
- Aquatic toxicology (Amsterdam, Netherlands) [ 0166-445X ] ; 2005.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Chromatography, Affinity, Chromatography, High Pressure Liquid, Chromatography, Liquid, Computational Biology, Cytosol (chemistry), Electrophoresis, Fishes (metabolism), Glutathione Transferase (chemistry), Glutathione Transferase (genetics), Immunoblotting, Mass Spectrometry, Molecular Sequence Data, Sequence Analysis, DNA.
- MESH :
- chemical , chemistry : Glutathione Transferase.
- chemistry : Cytosol.
- chemical , genetics : Glutathione Transferase.
- metabolism : Fishes.
- Amino Acid Sequence, Animals, Chromatography, Affinity, Chromatography, High Pressure Liquid, Chromatography, Liquid, Computational Biology, Electrophoresis, Immunoblotting, Mass Spectrometry, Molecular Sequence Data, Sequence Analysis, DNA.
Abstract
Glutathione S-transferases (GSTs) are a family of detoxification enzymes that catalyze the conjugation of glutathione (GSH) to electrophiles, thus preventing toxicity. This study characterized the cytosolic GST classes of juvenile white sturgeon (Acipenser transmontanus) liver, using two methods of isolation. The first, which employed affinity chromatography, electrophoresis and immunoblotting against a polyclonal striped bass GST antibody, yielded two cytosolic GSTs. The GSTs were identified by nanospray liquid chromatography-tandem mass spectrometry (LC-MS/MS), peptide mass mapping and MS/MS sequencing, as well as de novo MS/MS sequencing as GST classes pi and mu using the Mascot search engine and the NCBI non-redundant database (nrDB) for both methods. The molecular masses were determined to be 23,548 +/- 23 and 26,027 +/- 23 Da, respectively, using linear matrix assisted laser desorption ionization time of flight (MALDI-TOF) mass spectrometry. The second method of isolation, which used affinity chromatography and high-pressure liquid chromatography (HPLC), yielded pi, mu, and possibly two alpha isoforms by MALDI-TOF-TOF, again searching against the NCBI nrDB. The alpha isoforms were determined to have molecular masses of 25,528 +/- 23 and 25,348 +/- 23 Da by electrospray ionization source (ESI)-MS. Overall, it appears that the HPLC method is more sensitive than immunoblotting with the current antibody. Activity of the cytosolic GSTs was evaluated using the substrate 1-chloro-2,4-dinitrobenzene (CDNB) and found to be 2.4 +/- 0.6 U/mg cytosolic protein, and 0.41 +/- 0.05 U/mg cytosolic protein using ethacrynic acid (ETHA).
DOI: 10.1016/j.aquatox.2004.11.026
PubMed: 15670627
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pubmed:15670627Le document en format XML
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Burns</name></author><author><name sortKey="Mitchell, Alyson E" sort="Mitchell, Alyson E" uniqKey="Mitchell A" first="Alyson E" last="Mitchell">Alyson E. Mitchell</name></author><author><name sortKey="Lame, M W" sort="Lame, M W" uniqKey="Lame M" first="M W" last="Lamé">M W Lamé</name></author><author><name sortKey="Segall, H J" sort="Segall, H J" uniqKey="Segall H" first="H J" last="Segall">H J Segall</name></author><author><name sortKey="Tjeerdema, Ronald S" sort="Tjeerdema, Ronald S" uniqKey="Tjeerdema R" first="Ronald S" last="Tjeerdema">Ronald S. 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Donham</name><affiliation><nlm:affiliation>Department of Environmental Toxicology, College of Agricultural and Environmental Sciences, University of California, 1 Shields Avenue, Davis, CA 95616-8588, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Morin, Dexter" sort="Morin, Dexter" uniqKey="Morin D" first="Dexter" last="Morin">Dexter Morin</name></author><author><name sortKey="Jewell, William T" sort="Jewell, William T" uniqKey="Jewell W" first="William T" last="Jewell">William T. Jewell</name></author><author><name sortKey="Burns, Stephanie A" sort="Burns, Stephanie A" uniqKey="Burns S" first="Stephanie A" last="Burns">Stephanie A. Burns</name></author><author><name sortKey="Mitchell, Alyson E" sort="Mitchell, Alyson E" uniqKey="Mitchell A" first="Alyson E" last="Mitchell">Alyson E. Mitchell</name></author><author><name sortKey="Lame, M W" sort="Lame, M W" uniqKey="Lame M" first="M W" last="Lamé">M W Lamé</name></author><author><name sortKey="Segall, H J" sort="Segall, H J" uniqKey="Segall H" first="H J" last="Segall">H J Segall</name></author><author><name sortKey="Tjeerdema, Ronald S" sort="Tjeerdema, Ronald S" uniqKey="Tjeerdema R" first="Ronald S" last="Tjeerdema">Ronald S. Tjeerdema</name></author></analytic><series><title level="j">Aquatic toxicology (Amsterdam, Netherlands)</title><idno type="ISSN">0166-445X</idno><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Chromatography, Affinity</term><term>Chromatography, High Pressure Liquid</term><term>Chromatography, Liquid</term><term>Computational Biology</term><term>Cytosol (chemistry)</term><term>Electrophoresis</term><term>Fishes (metabolism)</term><term>Glutathione Transferase (chemistry)</term><term>Glutathione Transferase (genetics)</term><term>Immunoblotting</term><term>Mass Spectrometry</term><term>Molecular Sequence Data</term><term>Sequence Analysis, DNA</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutathione Transferase</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Cytosol</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutathione Transferase</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Fishes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Chromatography, Affinity</term><term>Chromatography, High Pressure Liquid</term><term>Chromatography, Liquid</term><term>Computational Biology</term><term>Electrophoresis</term><term>Immunoblotting</term><term>Mass Spectrometry</term><term>Molecular Sequence Data</term><term>Sequence Analysis, DNA</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutathione S-transferases (GSTs) are a family of detoxification enzymes that catalyze the conjugation of glutathione (GSH) to electrophiles, thus preventing toxicity. This study characterized the cytosolic GST classes of juvenile white sturgeon (Acipenser transmontanus) liver, using two methods of isolation. The first, which employed affinity chromatography, electrophoresis and immunoblotting against a polyclonal striped bass GST antibody, yielded two cytosolic GSTs. The GSTs were identified by nanospray liquid chromatography-tandem mass spectrometry (LC-MS/MS), peptide mass mapping and MS/MS sequencing, as well as de novo MS/MS sequencing as GST classes pi and mu using the Mascot search engine and the NCBI non-redundant database (nrDB) for both methods. The molecular masses were determined to be 23,548 +/- 23 and 26,027 +/- 23 Da, respectively, using linear matrix assisted laser desorption ionization time of flight (MALDI-TOF) mass spectrometry. The second method of isolation, which used affinity chromatography and high-pressure liquid chromatography (HPLC), yielded pi, mu, and possibly two alpha isoforms by MALDI-TOF-TOF, again searching against the NCBI nrDB. The alpha isoforms were determined to have molecular masses of 25,528 +/- 23 and 25,348 +/- 23 Da by electrospray ionization source (ESI)-MS. Overall, it appears that the HPLC method is more sensitive than immunoblotting with the current antibody. Activity of the cytosolic GSTs was evaluated using the substrate 1-chloro-2,4-dinitrobenzene (CDNB) and found to be 2.4 +/- 0.6 U/mg cytosolic protein, and 0.41 +/- 0.05 U/mg cytosolic protein using ethacrynic acid (ETHA).</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15670627</PMID><DateCreated><Year>2005</Year><Month>01</Month><Day>26</Day></DateCreated><DateCompleted><Year>2005</Year><Month>04</Month><Day>12</Day></DateCompleted><DateRevised><Year>2006</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0166-445X</ISSN><JournalIssue CitedMedium="Print"><Volume>71</Volume><Issue>3</Issue><PubDate><Year>2005</Year><Month>Feb</Month><Day>10</Day></PubDate></JournalIssue><Title>Aquatic toxicology (Amsterdam, Netherlands)</Title><ISOAbbreviation>Aquat. Toxicol.</ISOAbbreviation></Journal><ArticleTitle>Characterization of glutathione S-transferases in juvenile white sturgeon.</ArticleTitle><Pagination><MedlinePgn>203-14</MedlinePgn></Pagination><Abstract><AbstractText>Glutathione S-transferases (GSTs) are a family of detoxification enzymes that catalyze the conjugation of glutathione (GSH) to electrophiles, thus preventing toxicity. This study characterized the cytosolic GST classes of juvenile white sturgeon (Acipenser transmontanus) liver, using two methods of isolation. The first, which employed affinity chromatography, electrophoresis and immunoblotting against a polyclonal striped bass GST antibody, yielded two cytosolic GSTs. The GSTs were identified by nanospray liquid chromatography-tandem mass spectrometry (LC-MS/MS), peptide mass mapping and MS/MS sequencing, as well as de novo MS/MS sequencing as GST classes pi and mu using the Mascot search engine and the NCBI non-redundant database (nrDB) for both methods. The molecular masses were determined to be 23,548 +/- 23 and 26,027 +/- 23 Da, respectively, using linear matrix assisted laser desorption ionization time of flight (MALDI-TOF) mass spectrometry. The second method of isolation, which used affinity chromatography and high-pressure liquid chromatography (HPLC), yielded pi, mu, and possibly two alpha isoforms by MALDI-TOF-TOF, again searching against the NCBI nrDB. The alpha isoforms were determined to have molecular masses of 25,528 +/- 23 and 25,348 +/- 23 Da by electrospray ionization source (ESI)-MS. Overall, it appears that the HPLC method is more sensitive than immunoblotting with the current antibody. Activity of the cytosolic GSTs was evaluated using the substrate 1-chloro-2,4-dinitrobenzene (CDNB) and found to be 2.4 +/- 0.6 U/mg cytosolic protein, and 0.41 +/- 0.05 U/mg cytosolic protein using ethacrynic acid (ETHA).</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Donham</LastName><ForeName>Rachel T</ForeName><Initials>RT</Initials><AffiliationInfo><Affiliation>Department of Environmental Toxicology, College of Agricultural and Environmental Sciences, University of California, 1 Shields Avenue, Davis, CA 95616-8588, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Morin</LastName><ForeName>Dexter</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Jewell</LastName><ForeName>William T</ForeName><Initials>WT</Initials></Author><Author ValidYN="Y"><LastName>Burns</LastName><ForeName>Stephanie A</ForeName><Initials>SA</Initials></Author><Author ValidYN="Y"><LastName>Mitchell</LastName><ForeName>Alyson E</ForeName><Initials>AE</Initials></Author><Author ValidYN="Y"><LastName>Lamé</LastName><ForeName>M W</ForeName><Initials>MW</Initials></Author><Author ValidYN="Y"><LastName>Segall</LastName><ForeName>H J</ForeName><Initials>HJ</Initials></Author><Author ValidYN="Y"><LastName>Tjeerdema</LastName><ForeName>Ronald S</ForeName><Initials>RS</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2005</Year><Month>01</Month><Day>17</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Aquat Toxicol</MedlineTA><NlmUniqueID>8500246</NlmUniqueID><ISSNLinking>0166-445X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>EC 2.5.1.18</RegistryNumber><NameOfSubstance UI="D005982">Glutathione Transferase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002846" MajorTopicYN="N">Chromatography, Affinity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002851" MajorTopicYN="N">Chromatography, High Pressure Liquid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002853" MajorTopicYN="N">Chromatography, Liquid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019295" MajorTopicYN="N">Computational Biology</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003600" MajorTopicYN="N">Cytosol</DescriptorName><QualifierName UI="Q000737" 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