EsturgeonV1, Main, Exploration, bibRecord, 000F90

Characterization of glutathione S-transferases in juvenile white sturgeon

Identifieur interne : 000F90 ( Main/Exploration ); précédent : 000F89; suivant : 000F91

Characterization of glutathione S-transferases in juvenile white sturgeon

Auteurs : Rachel T. Donham [États-Unis] ; Dexter Morin [États-Unis] ; William T. Jewell [États-Unis] ; Stephanie A. Burns [États-Unis] ; Alyson E. Mitchell [États-Unis] ; M. W. Lame [États-Unis] ; H. J. Segall [États-Unis] ; Ronald S. Tjeerdema [États-Unis]

Source :

Aquatic toxicology [ 0166-445X ] ; 2005.

RBID : Pascal:05-0148244

Descripteurs français

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

English descriptors

KwdEn :
- Acipenser transmontanus, Amino Acid Sequence, Animals, Aquatic environment, Characterization, Chromatography, Affinity, Chromatography, High Pressure Liquid, Chromatography, Liquid, Computational Biology, Cytosol (chemistry), Ecotoxicology, Electrophoresis, Fishes (metabolism), Glutathione Transferase (chemistry), Glutathione Transferase (genetics), Glutathione transferase, 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 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).

Affiliations:

Le document en format XML

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<term>Characterization</term>
<term>Chromatography, Affinity</term>
<term>Chromatography, High Pressure Liquid</term>
<term>Chromatography, Liquid</term>
<term>Computational Biology</term>
<term>Cytosol (chemistry)</term>
<term>Ecotoxicology</term>
<term>Electrophoresis</term>
<term>Fishes (metabolism)</term>
<term>Glutathione Transferase (chemistry)</term>
<term>Glutathione Transferase (genetics)</term>
<term>Glutathione transferase</term>
<term>Immunoblotting</term>
<term>Mass Spectrometry</term>
<term>Molecular Sequence Data</term>
<term>Sequence Analysis, DNA</term>
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<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Cytosol</term>
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<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>
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<term>Milieu aquatique</term>
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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>
</front>
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<affiliations><list><country><li>États-Unis</li>
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<tree><country name="États-Unis"><region name="Californie"><name sortKey="Donham, Rachel T" sort="Donham, Rachel T" uniqKey="Donham R" first="Rachel T." last="Donham">Rachel T. Donham</name>
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<name sortKey="Burns, Stephanie A" sort="Burns, Stephanie A" uniqKey="Burns S" first="Stephanie A." last="Burns">Stephanie A. Burns</name>
<name sortKey="Jewell, William T" sort="Jewell, William T" uniqKey="Jewell W" first="William T." last="Jewell">William T. Jewell</name>
<name sortKey="Lame, M W" sort="Lame, M W" uniqKey="Lame M" first="M. W." last="Lame">M. W. Lame</name>
<name sortKey="Mitchell, Alyson E" sort="Mitchell, Alyson E" uniqKey="Mitchell A" first="Alyson E." last="Mitchell">Alyson E. Mitchell</name>
<name sortKey="Morin, Dexter" sort="Morin, Dexter" uniqKey="Morin D" first="Dexter" last="Morin">Dexter Morin</name>
<name sortKey="Segall, H J" sort="Segall, H J" uniqKey="Segall H" first="H. J." last="Segall">H. J. Segall</name>
<name sortKey="Tjeerdema, Ronald S" sort="Tjeerdema, Ronald S" uniqKey="Tjeerdema R" first="Ronald S." last="Tjeerdema">Ronald S. Tjeerdema</name>
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Characterization of glutathione S-transferases in juvenile white sturgeon

Characterization of glutathione S-transferases in juvenile white sturgeon

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

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