A new thioredoxin reductase with additional glutathione reductase activity in Haemonchus contortus.
Identifieur interne : 000395 ( Main/Exploration ); précédent : 000394; suivant : 000396A new thioredoxin reductase with additional glutathione reductase activity in Haemonchus contortus.
Auteurs : Agustín Plancarte [Mexique] ; Gabriela Nava [Mexique] ; Javier A. Munguía [Mexique]Source :
- Experimental parasitology [ 1090-2449 ] ; 2017.
Descripteurs français
- KwdFr :
- 5,5'-Dithiobis(acide 2-nitro-benzoïque) (métabolisme), Abomasum (parasitologie), Alignement de séquences (MeSH), Animaux (MeSH), Azoles (métabolisme), Capra (MeSH), Cinétique (MeSH), Composés organiques du sélénium (métabolisme), Concentration en ions d'hydrogène (MeSH), Disulfure de glutathion (métabolisme), Glutathione reductase (composition chimique), Glutathione reductase (isolement et purification), Glutathione reductase (métabolisme), Haemonchus (enzymologie), Infections à Haemonchus (médecine vétérinaire), Infections à Haemonchus (parasitologie), Maladies des chèvres (parasitologie), Maladies des ovins (parasitologie), NADP (métabolisme), Ovis (MeSH), S-Nitroso-glutathion (métabolisme), Spécificité du substrat (MeSH), Sélénite de sodium (métabolisme), Séquence d'acides aminés (MeSH), Température (MeSH), Thioredoxin-disulfide reductase (composition chimique), Thioredoxin-disulfide reductase (isolement et purification), Thioredoxin-disulfide reductase (métabolisme).
- MESH :
- composition chimique : Glutathione reductase, Thioredoxin-disulfide reductase.
- enzymologie : Haemonchus.
- isolement et purification : Glutathione reductase, Thioredoxin-disulfide reductase.
- médecine vétérinaire : Infections à Haemonchus.
- métabolisme : 5,5'-Dithiobis(acide 2-nitro-benzoïque), Azoles, Composés organiques du sélénium, Disulfure de glutathion, Glutathione reductase, NADP, S-Nitroso-glutathion, Sélénite de sodium, Thioredoxin-disulfide reductase.
- parasitologie : Abomasum, Infections à Haemonchus, Maladies des chèvres, Maladies des ovins.
- Alignement de séquences, Animaux, Capra, Cinétique, Concentration en ions d'hydrogène, Ovis, Spécificité du substrat, Séquence d'acides aminés, Température.
English descriptors
- KwdEn :
- Abomasum (parasitology), Amino Acid Sequence (MeSH), Animals (MeSH), Azoles (metabolism), Dithionitrobenzoic Acid (metabolism), Glutathione Disulfide (metabolism), Glutathione Reductase (chemistry), Glutathione Reductase (isolation & purification), Glutathione Reductase (metabolism), Goat Diseases (parasitology), Goats (MeSH), Haemonchiasis (parasitology), Haemonchiasis (veterinary), Haemonchus (enzymology), Hydrogen-Ion Concentration (MeSH), Kinetics (MeSH), NADP (metabolism), Organoselenium Compounds (metabolism), S-Nitrosoglutathione (metabolism), Sequence Alignment (MeSH), Sheep (MeSH), Sheep Diseases (parasitology), Sodium Selenite (metabolism), Substrate Specificity (MeSH), Temperature (MeSH), Thioredoxin-Disulfide Reductase (chemistry), Thioredoxin-Disulfide Reductase (isolation & purification), Thioredoxin-Disulfide Reductase (metabolism).
- MESH :
- chemical , chemistry : Glutathione Reductase, Thioredoxin-Disulfide Reductase.
- chemical , isolation & purification : Glutathione Reductase, Thioredoxin-Disulfide Reductase.
- chemical , metabolism : Azoles, Dithionitrobenzoic Acid, Glutathione Disulfide, Glutathione Reductase, NADP, Organoselenium Compounds, S-Nitrosoglutathione, Sodium Selenite, Thioredoxin-Disulfide Reductase.
- enzymology : Haemonchus.
- parasitology : Abomasum, Goat Diseases, Haemonchiasis, Sheep Diseases.
- veterinary : Haemonchiasis.
- Amino Acid Sequence, Animals, Goats, Hydrogen-Ion Concentration, Kinetics, Sequence Alignment, Sheep, Substrate Specificity, Temperature.
Abstract
We report, herein, the purification to homogeneity and the biochemical and kinetic characterization of HcTrxR3, a new isoform of thioredoxin reductase (TrxR) from Haemonchus contortus. HcTrxR3 was found to have a relative molecular weight of 134,000, while the corresponding value per subunit obtained under denaturing conditions, was of 67,000. By peptide mass spectrophotometric analysis, HcTrxR3 was determined to have 99% identity with the H. contortus HcTrxR1 although, and most importantly, they are different in their amino acid sequence in two amino acid positions: 48 (isoleucine instead of leucine) and 460 (leucine instead of proline). The enzyme catalyzes NADPH-dependent reduction of DTNB and, unexpectedly, it follows the pattern of glutathione reductases (GR) performing the reduction of oxidized glutathione (GSSG) to reduced glutathione using NADPH as the reducing cofactor. Hence, it is important to highlight this enzyme's new and unexpected condition that makes so special and one our main finding. Enzyme Kcat values for DTNB, GSSG and NADPH were 12, 3 and 8 s-1, respectively. HcTrxR3 developed, into specific TrxR substrates: ebselen and sodium selenite, with activity at 0.5 and 0.068 (U/mg), respectively; and 0.044 (U/mg) for S-nitrosoglutathione through its GR activity. The enzyme was inhibited by gold compound auranofin (AU), a selective inhibitor of thiol-dependent flavoreductases. Although HcTrxR3 has both TrxR and GR activity as thioredoxin glutathione reductase (TGR) does, it is a TrxR because it has no glutaredoxin domain and it does not develop any hysteretic behavior as does TGR. The importance of this new enzyme is potential to further clarify the detoxification and haemostasis redox mechanism in H. contortus. Likewise, this enzyme could also be a protein model to recognize more differences between TrxR and GR.
DOI: 10.1016/j.exppara.2017.04.006
PubMed: 28456691
Affiliations:
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(chemistry)</term><term>Glutathione Reductase (isolation & purification)</term><term>Glutathione Reductase (metabolism)</term><term>Goat Diseases (parasitology)</term><term>Goats (MeSH)</term><term>Haemonchiasis (parasitology)</term><term>Haemonchiasis (veterinary)</term><term>Haemonchus (enzymology)</term><term>Hydrogen-Ion Concentration (MeSH)</term><term>Kinetics (MeSH)</term><term>NADP (metabolism)</term><term>Organoselenium Compounds (metabolism)</term><term>S-Nitrosoglutathione (metabolism)</term><term>Sequence Alignment (MeSH)</term><term>Sheep (MeSH)</term><term>Sheep Diseases (parasitology)</term><term>Sodium Selenite (metabolism)</term><term>Substrate Specificity (MeSH)</term><term>Temperature (MeSH)</term><term>Thioredoxin-Disulfide Reductase (chemistry)</term><term>Thioredoxin-Disulfide Reductase (isolation & purification)</term><term>Thioredoxin-Disulfide Reductase (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>5,5'-Dithiobis(acide 2-nitro-benzoïque) (métabolisme)</term><term>Abomasum (parasitologie)</term><term>Alignement de séquences (MeSH)</term><term>Animaux (MeSH)</term><term>Azoles (métabolisme)</term><term>Capra (MeSH)</term><term>Cinétique (MeSH)</term><term>Composés organiques du sélénium (métabolisme)</term><term>Concentration en ions d'hydrogène (MeSH)</term><term>Disulfure de glutathion (métabolisme)</term><term>Glutathione reductase (composition chimique)</term><term>Glutathione reductase (isolement et purification)</term><term>Glutathione reductase (métabolisme)</term><term>Haemonchus (enzymologie)</term><term>Infections à Haemonchus (médecine vétérinaire)</term><term>Infections à Haemonchus (parasitologie)</term><term>Maladies des chèvres (parasitologie)</term><term>Maladies des ovins (parasitologie)</term><term>NADP (métabolisme)</term><term>Ovis (MeSH)</term><term>S-Nitroso-glutathion (métabolisme)</term><term>Spécificité du substrat (MeSH)</term><term>Sélénite de sodium (métabolisme)</term><term>Séquence d'acides aminés (MeSH)</term><term>Température (MeSH)</term><term>Thioredoxin-disulfide reductase (composition chimique)</term><term>Thioredoxin-disulfide reductase (isolement et purification)</term><term>Thioredoxin-disulfide reductase (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutathione Reductase</term><term>Thioredoxin-Disulfide Reductase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Glutathione Reductase</term><term>Thioredoxin-Disulfide Reductase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Azoles</term><term>Dithionitrobenzoic Acid</term><term>Glutathione Disulfide</term><term>Glutathione Reductase</term><term>NADP</term><term>Organoselenium Compounds</term><term>S-Nitrosoglutathione</term><term>Sodium Selenite</term><term>Thioredoxin-Disulfide Reductase</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glutathione reductase</term><term>Thioredoxin-disulfide reductase</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Haemonchus</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Haemonchus</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Glutathione reductase</term><term>Thioredoxin-disulfide reductase</term></keywords><keywords scheme="MESH" qualifier="médecine vétérinaire" xml:lang="fr"><term>Infections à Haemonchus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>5,5'-Dithiobis(acide 2-nitro-benzoïque)</term><term>Azoles</term><term>Composés organiques du sélénium</term><term>Disulfure de glutathion</term><term>Glutathione reductase</term><term>NADP</term><term>S-Nitroso-glutathion</term><term>Sélénite de sodium</term><term>Thioredoxin-disulfide reductase</term></keywords><keywords scheme="MESH" qualifier="parasitologie" xml:lang="fr"><term>Abomasum</term><term>Infections à Haemonchus</term><term>Maladies des chèvres</term><term>Maladies des ovins</term></keywords><keywords scheme="MESH" qualifier="parasitology" xml:lang="en"><term>Abomasum</term><term>Goat Diseases</term><term>Haemonchiasis</term><term>Sheep Diseases</term></keywords><keywords scheme="MESH" qualifier="veterinary" xml:lang="en"><term>Haemonchiasis</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Goats</term><term>Hydrogen-Ion Concentration</term><term>Kinetics</term><term>Sequence Alignment</term><term>Sheep</term><term>Substrate Specificity</term><term>Temperature</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Animaux</term><term>Capra</term><term>Cinétique</term><term>Concentration en ions d'hydrogène</term><term>Ovis</term><term>Spécificité du substrat</term><term>Séquence d'acides aminés</term><term>Température</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We report, herein, the purification to homogeneity and the biochemical and kinetic characterization of HcTrxR3, a new isoform of thioredoxin reductase (TrxR) from Haemonchus contortus. HcTrxR3 was found to have a relative molecular weight of 134,000, while the corresponding value per subunit obtained under denaturing conditions, was of 67,000. By peptide mass spectrophotometric analysis, HcTrxR3 was determined to have 99% identity with the H. contortus HcTrxR1 although, and most importantly, they are different in their amino acid sequence in two amino acid positions: 48 (isoleucine instead of leucine) and 460 (leucine instead of proline). The enzyme catalyzes NADPH-dependent reduction of DTNB and, unexpectedly, it follows the pattern of glutathione reductases (GR) performing the reduction of oxidized glutathione (GSSG) to reduced glutathione using NADPH as the reducing cofactor. Hence, it is important to highlight this enzyme's new and unexpected condition that makes so special and one our main finding. Enzyme K<sub>cat</sub> values for DTNB, GSSG and NADPH were 12, 3 and 8 s<sup>-1</sup>, respectively. HcTrxR3 developed, into specific TrxR substrates: ebselen and sodium selenite, with activity at 0.5 and 0.068 (U/mg), respectively; and 0.044 (U/mg) for S-nitrosoglutathione through its GR activity. The enzyme was inhibited by gold compound auranofin (AU), a selective inhibitor of thiol-dependent flavoreductases. Although HcTrxR3 has both TrxR and GR activity as thioredoxin glutathione reductase (TGR) does, it is a TrxR because it has no glutaredoxin domain and it does not develop any hysteretic behavior as does TGR. The importance of this new enzyme is potential to further clarify the detoxification and haemostasis redox mechanism in H. contortus. Likewise, this enzyme could also be a protein model to recognize more differences between TrxR and GR.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28456691</PMID><DateCompleted><Year>2017</Year><Month>06</Month><Day>20</Day></DateCompleted><DateRevised><Year>2017</Year><Month>06</Month><Day>20</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1090-2449</ISSN><JournalIssue CitedMedium="Internet"><Volume>177</Volume><PubDate><Year>2017</Year><Month>Jun</Month></PubDate></JournalIssue><Title>Experimental parasitology</Title><ISOAbbreviation>Exp Parasitol</ISOAbbreviation></Journal><ArticleTitle>A new thioredoxin reductase with additional glutathione reductase activity in Haemonchus contortus.</ArticleTitle><Pagination><MedlinePgn>82-92</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0014-4894(16)30255-7</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.exppara.2017.04.006</ELocationID><Abstract><AbstractText>We report, herein, the purification to homogeneity and the biochemical and kinetic characterization of HcTrxR3, a new isoform of thioredoxin reductase (TrxR) from Haemonchus contortus. HcTrxR3 was found to have a relative molecular weight of 134,000, while the corresponding value per subunit obtained under denaturing conditions, was of 67,000. By peptide mass spectrophotometric analysis, HcTrxR3 was determined to have 99% identity with the H. contortus HcTrxR1 although, and most importantly, they are different in their amino acid sequence in two amino acid positions: 48 (isoleucine instead of leucine) and 460 (leucine instead of proline). The enzyme catalyzes NADPH-dependent reduction of DTNB and, unexpectedly, it follows the pattern of glutathione reductases (GR) performing the reduction of oxidized glutathione (GSSG) to reduced glutathione using NADPH as the reducing cofactor. Hence, it is important to highlight this enzyme's new and unexpected condition that makes so special and one our main finding. Enzyme K<sub>cat</sub> values for DTNB, GSSG and NADPH were 12, 3 and 8 s<sup>-1</sup>, respectively. HcTrxR3 developed, into specific TrxR substrates: ebselen and sodium selenite, with activity at 0.5 and 0.068 (U/mg), respectively; and 0.044 (U/mg) for S-nitrosoglutathione through its GR activity. The enzyme was inhibited by gold compound auranofin (AU), a selective inhibitor of thiol-dependent flavoreductases. Although HcTrxR3 has both TrxR and GR activity as thioredoxin glutathione reductase (TGR) does, it is a TrxR because it has no glutaredoxin domain and it does not develop any hysteretic behavior as does TGR. The importance of this new enzyme is potential to further clarify the detoxification and haemostasis redox mechanism in H. contortus. Likewise, this enzyme could also be a protein model to recognize more differences between TrxR and GR.</AbstractText><CopyrightInformation>Copyright © 2017 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Plancarte</LastName><ForeName>Agustín</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Departamento de Microbiología y Parasitología, Facultad de Medicina, Universidad Nacional Autónoma de México, UNAM, Ciudad de México, 04510, Mexico. Electronic address: apc@unam.mx.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nava</LastName><ForeName>Gabriela</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Departamento de Microbiología y Parasitología, Facultad de Medicina, Universidad Nacional Autónoma de México, UNAM, Ciudad de México, 04510, Mexico.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Munguía</LastName><ForeName>Javier A</ForeName><Initials>JA</Initials><AffiliationInfo><Affiliation>Departamento de Ciencias Agronómicas y Veterinarias, Instituto Tecnológico de Sonora, 85000 Ciudad Obregón, Sonora, Mexico.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>04</Month><Day>26</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Exp Parasitol</MedlineTA><NlmUniqueID>0370713</NlmUniqueID><ISSNLinking>0014-4894</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001393">Azoles</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D016566">Organoselenium Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>40X2P7DPGH</RegistryNumber><NameOfSubstance UI="C042986">ebselen</NameOfSubstance></Chemical><Chemical><RegistryNumber>53-59-8</RegistryNumber><NameOfSubstance UI="D009249">NADP</NameOfSubstance></Chemical><Chemical><RegistryNumber>57564-91-7</RegistryNumber><NameOfSubstance UI="D026422">S-Nitrosoglutathione</NameOfSubstance></Chemical><Chemical><RegistryNumber>9BZQ3U62JX</RegistryNumber><NameOfSubstance UI="D004228">Dithionitrobenzoic Acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.1.7</RegistryNumber><NameOfSubstance UI="D005980">Glutathione Reductase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.1.9</RegistryNumber><NameOfSubstance UI="D013880">Thioredoxin-Disulfide Reductase</NameOfSubstance></Chemical><Chemical><RegistryNumber>HIW548RQ3W</RegistryNumber><NameOfSubstance UI="D018038">Sodium Selenite</NameOfSubstance></Chemical><Chemical><RegistryNumber>ULW86O013H</RegistryNumber><NameOfSubstance UI="D019803">Glutathione Disulfide</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000018" MajorTopicYN="N">Abomasum</DescriptorName><QualifierName UI="Q000469" MajorTopicYN="N">parasitology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001393" MajorTopicYN="N">Azoles</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004228" MajorTopicYN="N">Dithionitrobenzoic Acid</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019803" MajorTopicYN="N">Glutathione Disulfide</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005980" MajorTopicYN="N">Glutathione Reductase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015511" MajorTopicYN="N">Goat Diseases</DescriptorName><QualifierName UI="Q000469" MajorTopicYN="N">parasitology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006041" MajorTopicYN="N">Goats</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006188" MajorTopicYN="N">Haemonchiasis</DescriptorName><QualifierName UI="Q000469" MajorTopicYN="N">parasitology</QualifierName><QualifierName UI="Q000662" MajorTopicYN="N">veterinary</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006189" MajorTopicYN="N">Haemonchus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009249" MajorTopicYN="N">NADP</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016566" MajorTopicYN="N">Organoselenium Compounds</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D026422" MajorTopicYN="N">S-Nitrosoglutathione</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012756" MajorTopicYN="N">Sheep</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012757" MajorTopicYN="N">Sheep Diseases</DescriptorName><QualifierName UI="Q000469" MajorTopicYN="N">parasitology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018038" MajorTopicYN="N">Sodium Selenite</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013696" MajorTopicYN="N">Temperature</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013880" MajorTopicYN="N">Thioredoxin-Disulfide Reductase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Glutathione system</Keyword><Keyword MajorTopicYN="N">Haemonchosis</Keyword><Keyword MajorTopicYN="N">Helminthes</Keyword><Keyword MajorTopicYN="N">Kinetic</Keyword><Keyword MajorTopicYN="N">Redox-systems</Keyword><Keyword MajorTopicYN="N">Thioredoxin system</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2016</Year><Month>10</Month><Day>17</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2017</Year><Month>03</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2017</Year><Month>04</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2017</Year><Month>5</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2017</Year><Month>6</Month><Day>21</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2017</Year><Month>5</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">28456691</ArticleId><ArticleId IdType="pii">S0014-4894(16)30255-7</ArticleId><ArticleId IdType="doi">10.1016/j.exppara.2017.04.006</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Mexique</li></country></list><tree><country name="Mexique"><noRegion><name sortKey="Plancarte, Agustin" sort="Plancarte, Agustin" uniqKey="Plancarte A" first="Agustín" last="Plancarte">Agustín Plancarte</name></noRegion><name sortKey="Munguia, Javier A" sort="Munguia, Javier A" uniqKey="Munguia J" first="Javier A" last="Munguía">Javier A. Munguía</name><name sortKey="Nava, Gabriela" sort="Nava, Gabriela" uniqKey="Nava G" first="Gabriela" last="Nava">Gabriela Nava</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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|wiki= Bois
|area= GlutaredoxinV1
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|clé= pubmed:28456691
|texte= A new thioredoxin reductase with additional glutathione reductase activity in Haemonchus contortus.
}}
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