EsturgeonV1, PascalFrancis, Corpus, bibRecord, 000250

Characterization of glutathione S-transferases in juvenile white sturgeon

Identifieur interne : 000250 ( PascalFrancis/Corpus ); précédent : 000249; suivant : 000251

Characterization 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. Lame ; H. J. Segall ; Ronald S. Tjeerdema

Source :

Aquatic toxicology [ 0166-445X ] ; 2005.

RBID : Pascal:05-0148244

Descripteurs français

Pascal (Inist)
- Caractérisation, Glutathione transferase, Milieu aquatique, Ecotoxicologie, Acipenser transmontanus.

English descriptors

KwdEn :
- Acipenser transmontanus, Aquatic environment, Characterization, Ecotoxicology, Glutathione transferase.

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 π and μ 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 π, μ, and possibly two a isoforms by MALDI-TOF-TOF, again searching against the NCBI nrDB. The a 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).

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

A01	`01`	`1`		`@0 0166-445X`
A02	`01`			`@0 AQTODG`
A03		`1`		`@0 Aquat. toxicol.`
A05				`@2 71`
A06				`@2 3`
A08	`01`	`1`	`ENG`	`@1 Characterization of glutathione S-transferases in juvenile white sturgeon`
A11	`01`	`1`		`@1 DONHAM (Rachel T.)`
A11	`02`	`1`		`@1 MORIN (Dexter)`
A11	`03`	`1`		`@1 JEWELL (William T.)`
A11	`04`	`1`		`@1 BURNS (Stephanie A.)`
A11	`05`	`1`		`@1 MITCHELL (Alyson E.)`
A11	`06`	`1`		`@1 LAME (M. W.)`
A11	`07`	`1`		`@1 SEGALL (H. J.)`
A11	`08`	`1`		`@1 TJEERDEMA (Ronald S.)`
A14	`01`			`@1 Department of Environmental Toxicology, College of Agricultural and Environmental Sciences, University of California, I Shields Avenue @2 Davis, CA 95616-8588 @3 USA @Z 1 aut. @Z 8 aut.`
A14	`02`			`@1 Department of Molecular Biosciences: School of Veterinary Medicine, University of California, I Shields Avenue @2 Davis, CA 95616 @3 USA @Z 2 aut. @Z 6 aut. @Z 7 aut.`
A14	`03`			`@1 Molecular Structure Facility, University of California, 1 Shields Avenue @2 Davis, CA 95616 @3 USA @Z 3 aut.`
A14	`04`			`@1 Department of Food Science and Nutrition, College of Agriculture and Environmental Sciences, University of California, 1 Shields Avenue @2 Davis, CA 95616-8588 @3 USA @Z 4 aut. @Z 5 aut.`
A20				`@1 203-214`
A21				`@1 2005`
A23	`01`			`@0 ENG`
A43	`01`			`@1 INIST @2 18841 @5 354000125946860010`
A44				`@0 0000 @1 © 2005 INIST-CNRS. All rights reserved.`
A45				`@0 27 ref.`
A47	`01`	`1`		`@0 05-0148244`
A60				`@1 P`
A61				`@0 A`
A64	`01`	`1`		`@0 Aquatic toxicology`
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C01	`01`		`ENG`	@0 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 π and μ 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 π, μ, and possibly two a isoforms by MALDI-TOF-TOF, again searching against the NCBI nrDB. The a 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).
C02	`01`	`X`		`@0 002A14D05A`
C03	`01`	`X`	`FRE`	`@0 Caractérisation @5 01`
C03	`01`	`X`	`ENG`	`@0 Characterization @5 01`
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C03	`02`	`X`	`FRE`	`@0 Glutathione transferase @2 FE @5 02`
C03	`02`	`X`	`ENG`	`@0 Glutathione transferase @2 FE @5 02`
C03	`02`	`X`	`SPA`	`@0 Glutathione transferase @2 FE @5 02`
C03	`03`	`X`	`FRE`	`@0 Milieu aquatique @5 03`
C03	`03`	`X`	`ENG`	`@0 Aquatic environment @5 03`
C03	`03`	`X`	`SPA`	`@0 Medio acuático @5 03`
C03	`04`	`X`	`FRE`	`@0 Ecotoxicologie @5 04`
C03	`04`	`X`	`ENG`	`@0 Ecotoxicology @5 04`
C03	`04`	`X`	`SPA`	`@0 Ecotoxicología @5 04`
C03	`05`	`X`	`FRE`	`@0 Acipenser transmontanus @2 NS @5 55`
C03	`05`	`X`	`ENG`	`@0 Acipenser transmontanus @2 NS @5 55`
C03	`05`	`X`	`SPA`	`@0 Acipenser transmontanus @2 NS @5 55`
C07	`01`	`X`	`FRE`	`@0 Transferases @2 FE`
C07	`01`	`X`	`ENG`	`@0 Transferases @2 FE`
C07	`01`	`X`	`SPA`	`@0 Transferases @2 FE`
C07	`02`	`X`	`FRE`	`@0 Enzyme @2 FE`
C07	`02`	`X`	`ENG`	`@0 Enzyme @2 FE`
C07	`02`	`X`	`SPA`	`@0 Enzima @2 FE`
C07	`03`	`X`	`FRE`	`@0 Pisces @2 NS @5 29`
C07	`03`	`X`	`ENG`	`@0 Pisces @2 NS @5 29`
C07	`03`	`X`	`SPA`	`@0 Pisces @2 NS @5 29`
C07	`04`	`X`	`FRE`	`@0 Vertebrata @2 NS`
C07	`04`	`X`	`ENG`	`@0 Vertebrata @2 NS`
C07	`04`	`X`	`SPA`	`@0 Vertebrata @2 NS`
C07	`05`	`X`	`FRE`	`@0 Acipenseridae @4 INC @5 70`
N21				`@1 101`
N44	`01`			`@1 OTO`
N82				`@1 OTO`

Format Inist (serveur)

NO :	PASCAL 05-0148244 INIST
ET :	Characterization of glutathione S-transferases in juvenile white sturgeon
AU :	DONHAM (Rachel T.); MORIN (Dexter); JEWELL (William T.); BURNS (Stephanie A.); MITCHELL (Alyson E.); LAME (M. W.); SEGALL (H. J.); TJEERDEMA (Ronald S.)
AF :	Department of Environmental Toxicology, College of Agricultural and Environmental Sciences, University of California, I Shields Avenue/Davis, CA 95616-8588/Etats-Unis (1 aut., 8 aut.); Department of Molecular Biosciences: School of Veterinary Medicine, University of California, I Shields Avenue/Davis, CA 95616/Etats-Unis (2 aut., 6 aut., 7 aut.); Molecular Structure Facility, University of California, 1 Shields Avenue/Davis, CA 95616/Etats-Unis (3 aut.); Department of Food Science and Nutrition, College of Agriculture and Environmental Sciences, University of California, 1 Shields Avenue/Davis, CA 95616-8588/Etats-Unis (4 aut., 5 aut.)
DT :	Publication en série; Niveau analytique
SO :	Aquatic toxicology; ISSN 0166-445X; Coden AQTODG; Pays-Bas; Da. 2005; Vol. 71; No. 3; Pp. 203-214; Bibl. 27 ref.
LA :	Anglais
EA :	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 π and μ 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 π, μ, and possibly two a isoforms by MALDI-TOF-TOF, again searching against the NCBI nrDB. The a 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).
CC :	002A14D05A
FD :	Caractérisation; Glutathione transferase; Milieu aquatique; Ecotoxicologie; Acipenser transmontanus
FG :	Transferases; Enzyme; Pisces; Vertebrata; Acipenseridae
ED :	Characterization; Glutathione transferase; Aquatic environment; Ecotoxicology; Acipenser transmontanus
EG :	Transferases; Enzyme; Pisces; Vertebrata
SD :	Caracterización; Glutathione transferase; Medio acuático; Ecotoxicología; Acipenser transmontanus
LO :	INIST-18841.354000125946860010
ID :	05-0148244

Links to Exploration step

Pascal:05-0148244

Le document en format XML

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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a">Characterization of glutathione S-transferases in juvenile white sturgeon</title>
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<author><name sortKey="Mitchell, Alyson E" sort="Mitchell, Alyson E" uniqKey="Mitchell A" first="Alyson E." last="Mitchell">Alyson E. Mitchell</name>
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<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 π and μ 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 π, μ, and possibly two a isoforms by MALDI-TOF-TOF, again searching against the NCBI nrDB. The a 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>
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<fA11 i1="01" i2="1"><s1>DONHAM (Rachel T.)</s1>
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<fA11 i1="02" i2="1"><s1>MORIN (Dexter)</s1>
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<fA11 i1="08" i2="1"><s1>TJEERDEMA (Ronald S.)</s1>
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<fA14 i1="01"><s1>Department of Environmental Toxicology, College of Agricultural and Environmental Sciences, University of California, I Shields Avenue</s1>
<s2>Davis, CA 95616-8588</s2>
<s3>USA</s3>
<sZ>1 aut.</sZ>
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<fA14 i1="02"><s1>Department of Molecular Biosciences: School of Veterinary Medicine, University of California, I Shields Avenue</s1>
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<fA14 i1="03"><s1>Molecular Structure Facility, University of California, 1 Shields Avenue</s1>
<s2>Davis, CA 95616</s2>
<s3>USA</s3>
<sZ>3 aut.</sZ>
</fA14>
<fA14 i1="04"><s1>Department of Food Science and Nutrition, College of Agriculture and Environmental Sciences, University of California, 1 Shields Avenue</s1>
<s2>Davis, CA 95616-8588</s2>
<s3>USA</s3>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
</fA14>
<fA20><s1>203-214</s1>
</fA20>
<fA21><s1>2005</s1>
</fA21>
<fA23 i1="01"><s0>ENG</s0>
</fA23>
<fA43 i1="01"><s1>INIST</s1>
<s2>18841</s2>
<s5>354000125946860010</s5>
</fA43>
<fA44><s0>0000</s0>
<s1>© 2005 INIST-CNRS. All rights reserved.</s1>
</fA44>
<fA45><s0>27 ref.</s0>
</fA45>
<fA47 i1="01" i2="1"><s0>05-0148244</s0>
</fA47>
<fA60><s1>P</s1>
</fA60>
<fA61><s0>A</s0>
</fA61>
<fA64 i1="01" i2="1"><s0>Aquatic toxicology</s0>
</fA64>
<fA66 i1="01"><s0>NLD</s0>
</fA66>
<fC01 i1="01" l="ENG"><s0>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 π and μ 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 π, μ, and possibly two a isoforms by MALDI-TOF-TOF, again searching against the NCBI nrDB. The a 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).</s0>
</fC01>
<fC02 i1="01" i2="X"><s0>002A14D05A</s0>
</fC02>
<fC03 i1="01" i2="X" l="FRE"><s0>Caractérisation</s0>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="ENG"><s0>Characterization</s0>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="SPA"><s0>Caracterización</s0>
<s5>01</s5>
</fC03>
<fC03 i1="02" i2="X" l="FRE"><s0>Glutathione transferase</s0>
<s2>FE</s2>
<s5>02</s5>
</fC03>
<fC03 i1="02" i2="X" l="ENG"><s0>Glutathione transferase</s0>
<s2>FE</s2>
<s5>02</s5>
</fC03>
<fC03 i1="02" i2="X" l="SPA"><s0>Glutathione transferase</s0>
<s2>FE</s2>
<s5>02</s5>
</fC03>
<fC03 i1="03" i2="X" l="FRE"><s0>Milieu aquatique</s0>
<s5>03</s5>
</fC03>
<fC03 i1="03" i2="X" l="ENG"><s0>Aquatic environment</s0>
<s5>03</s5>
</fC03>
<fC03 i1="03" i2="X" l="SPA"><s0>Medio acuático</s0>
<s5>03</s5>
</fC03>
<fC03 i1="04" i2="X" l="FRE"><s0>Ecotoxicologie</s0>
<s5>04</s5>
</fC03>
<fC03 i1="04" i2="X" l="ENG"><s0>Ecotoxicology</s0>
<s5>04</s5>
</fC03>
<fC03 i1="04" i2="X" l="SPA"><s0>Ecotoxicología</s0>
<s5>04</s5>
</fC03>
<fC03 i1="05" i2="X" l="FRE"><s0>Acipenser transmontanus</s0>
<s2>NS</s2>
<s5>55</s5>
</fC03>
<fC03 i1="05" i2="X" l="ENG"><s0>Acipenser transmontanus</s0>
<s2>NS</s2>
<s5>55</s5>
</fC03>
<fC03 i1="05" i2="X" l="SPA"><s0>Acipenser transmontanus</s0>
<s2>NS</s2>
<s5>55</s5>
</fC03>
<fC07 i1="01" i2="X" l="FRE"><s0>Transferases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="01" i2="X" l="ENG"><s0>Transferases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="01" i2="X" l="SPA"><s0>Transferases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="02" i2="X" l="FRE"><s0>Enzyme</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="02" i2="X" l="ENG"><s0>Enzyme</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="02" i2="X" l="SPA"><s0>Enzima</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="03" i2="X" l="FRE"><s0>Pisces</s0>
<s2>NS</s2>
<s5>29</s5>
</fC07>
<fC07 i1="03" i2="X" l="ENG"><s0>Pisces</s0>
<s2>NS</s2>
<s5>29</s5>
</fC07>
<fC07 i1="03" i2="X" l="SPA"><s0>Pisces</s0>
<s2>NS</s2>
<s5>29</s5>
</fC07>
<fC07 i1="04" i2="X" l="FRE"><s0>Vertebrata</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="04" i2="X" l="ENG"><s0>Vertebrata</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="04" i2="X" l="SPA"><s0>Vertebrata</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="05" i2="X" l="FRE"><s0>Acipenseridae</s0>
<s4>INC</s4>
<s5>70</s5>
</fC07>
<fN21><s1>101</s1>
</fN21>
<fN44 i1="01"><s1>OTO</s1>
</fN44>
<fN82><s1>OTO</s1>
</fN82>
</pA>
</standard>
<server><NO>PASCAL 05-0148244 INIST</NO>
<ET>Characterization of glutathione S-transferases in juvenile white sturgeon</ET>
<AU>DONHAM (Rachel T.); MORIN (Dexter); JEWELL (William T.); BURNS (Stephanie A.); MITCHELL (Alyson E.); LAME (M. W.); SEGALL (H. J.); TJEERDEMA (Ronald S.)</AU>
<AF>Department of Environmental Toxicology, College of Agricultural and Environmental Sciences, University of California, I Shields Avenue/Davis, CA 95616-8588/Etats-Unis (1 aut., 8 aut.); Department of Molecular Biosciences: School of Veterinary Medicine, University of California, I Shields Avenue/Davis, CA 95616/Etats-Unis (2 aut., 6 aut., 7 aut.); Molecular Structure Facility, University of California, 1 Shields Avenue/Davis, CA 95616/Etats-Unis (3 aut.); Department of Food Science and Nutrition, College of Agriculture and Environmental Sciences, University of California, 1 Shields Avenue/Davis, CA 95616-8588/Etats-Unis (4 aut., 5 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>Aquatic toxicology; ISSN 0166-445X; Coden AQTODG; Pays-Bas; Da. 2005; Vol. 71; No. 3; Pp. 203-214; Bibl. 27 ref.</SO>
<LA>Anglais</LA>
<EA>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 π and μ 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 π, μ, and possibly two a isoforms by MALDI-TOF-TOF, again searching against the NCBI nrDB. The a 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).</EA>
<CC>002A14D05A</CC>
<FD>Caractérisation; Glutathione transferase; Milieu aquatique; Ecotoxicologie; Acipenser transmontanus</FD>
<FG>Transferases; Enzyme; Pisces; Vertebrata; Acipenseridae</FG>
<ED>Characterization; Glutathione transferase; Aquatic environment; Ecotoxicology; Acipenser transmontanus</ED>
<EG>Transferases; Enzyme; Pisces; Vertebrata</EG>
<SD>Caracterización; Glutathione transferase; Medio acuático; Ecotoxicología; Acipenser transmontanus</SD>
<LO>INIST-18841.354000125946860010</LO>
<ID>05-0148244</ID>
</server>
</inist>
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Characterization of glutathione S-transferases in juvenile white sturgeon

Characterization of glutathione S-transferases in juvenile white sturgeon

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