Purification and properties of a new glutathione-dependent thiol:disulphide oxidoreductase from rat liver.
Identifieur interne : 001368 ( Main/Exploration ); précédent : 001367; suivant : 001369Purification and properties of a new glutathione-dependent thiol:disulphide oxidoreductase from rat liver.
Auteurs : M G Battelli ; E. LorenzoniSource :
- The Biochemical journal [ 0264-6021 ] ; 1982.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Biosynthèse des protéines (MeSH), Distribution tissulaire (MeSH), Disulfures (pharmacologie), Foie (enzymologie), Glutarédoxines (MeSH), Glutathion (pharmacologie), Lignées consanguines de rats (MeSH), Masse moléculaire (MeSH), Oxidoreductases (isolement et purification), Oxidoreductases (métabolisme), Protein-disulfide reductase (glutathione) (MeSH), Rats (MeSH), Ricine (pharmacologie), Techniques in vitro (MeSH), Xanthine dehydrogenase (métabolisme).
- MESH :
- enzymologie : Foie.
- isolement et purification : Oxidoreductases.
- métabolisme : Oxidoreductases, Xanthine dehydrogenase.
- pharmacologie : Disulfures, Glutathion, Ricine.
- Animaux, Biosynthèse des protéines, Distribution tissulaire, Glutarédoxines, Lignées consanguines de rats, Masse moléculaire, Protein-disulfide reductase (glutathione), Rats, Techniques in vitro.
English descriptors
- KwdEn :
- Animals (MeSH), Disulfides (pharmacology), Glutaredoxins (MeSH), Glutathione (pharmacology), In Vitro Techniques (MeSH), Liver (enzymology), Molecular Weight (MeSH), Oxidoreductases (isolation & purification), Oxidoreductases (metabolism), Protein Biosynthesis (MeSH), Protein Disulfide Reductase (Glutathione) (MeSH), Rats (MeSH), Rats, Inbred Strains (MeSH), Ricin (pharmacology), Tissue Distribution (MeSH), Xanthine Dehydrogenase (metabolism).
- MESH :
- chemical , isolation & purification : Oxidoreductases.
- chemical , metabolism : Oxidoreductases, Xanthine Dehydrogenase.
- chemical , pharmacology : Disulfides, Glutathione, Ricin.
- enzymology : Liver.
- Animals, Glutaredoxins, In Vitro Techniques, Molecular Weight, Protein Biosynthesis, Protein Disulfide Reductase (Glutathione), Rats, Rats, Inbred Strains, Tissue Distribution.
Abstract
A new GSSG-dependent thiol:disulphide oxidoreductase was extensively purified from rat liver cytosol. The enzymic protein shows molecular weight 40 000 as determined by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, and 43 000 as determined by thin-layer gel filtration on Bio-Gel P-100. The pI is 8.1. This enzyme converts rat liver xanthine dehydrogenase into an oxidase, in the presence of oxidized glutathione. Other disulphide compounds are either inactive or far less active than oxidized glutathione in the enzymic oxidation of rat liver xanthine dehydrogenase. The enzyme also catalyses the reduction of the disulphide bond of ricin and acts as a thioltransferase and as a GSH:insulin transhydrogenase. The enzymic activity was measured in various organs of newborn and adult rats.
DOI: 10.1042/bj2070133
PubMed: 6960894
PubMed Central: PMC1153833
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Purification and properties of a new glutathione-dependent thiol:disulphide oxidoreductase from rat liver.</title><author><name sortKey="Battelli, M G" sort="Battelli, M G" uniqKey="Battelli M" first="M G" last="Battelli">M G Battelli</name></author><author><name sortKey="Lorenzoni, E" sort="Lorenzoni, E" uniqKey="Lorenzoni E" first="E" last="Lorenzoni">E. Lorenzoni</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1982">1982</date><idno type="RBID">pubmed:6960894</idno><idno type="pmid">6960894</idno><idno type="pmc">PMC1153833</idno><idno type="doi">10.1042/bj2070133</idno><idno type="wicri:Area/Main/Corpus">001368</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001368</idno><idno type="wicri:Area/Main/Curation">001368</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001368</idno><idno type="wicri:Area/Main/Exploration">001368</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Purification and properties of a new glutathione-dependent thiol:disulphide oxidoreductase from rat liver.</title><author><name sortKey="Battelli, M G" sort="Battelli, M G" uniqKey="Battelli M" first="M G" last="Battelli">M G Battelli</name></author><author><name sortKey="Lorenzoni, E" sort="Lorenzoni, E" uniqKey="Lorenzoni E" first="E" last="Lorenzoni">E. Lorenzoni</name></author></analytic><series><title level="j">The Biochemical journal</title><idno type="ISSN">0264-6021</idno><imprint><date when="1982" type="published">1982</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Disulfides (pharmacology)</term><term>Glutaredoxins (MeSH)</term><term>Glutathione (pharmacology)</term><term>In Vitro Techniques (MeSH)</term><term>Liver (enzymology)</term><term>Molecular Weight (MeSH)</term><term>Oxidoreductases (isolation & purification)</term><term>Oxidoreductases (metabolism)</term><term>Protein Biosynthesis (MeSH)</term><term>Protein Disulfide Reductase (Glutathione) (MeSH)</term><term>Rats (MeSH)</term><term>Rats, Inbred Strains (MeSH)</term><term>Ricin (pharmacology)</term><term>Tissue Distribution (MeSH)</term><term>Xanthine Dehydrogenase (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Biosynthèse des protéines (MeSH)</term><term>Distribution tissulaire (MeSH)</term><term>Disulfures (pharmacologie)</term><term>Foie (enzymologie)</term><term>Glutarédoxines (MeSH)</term><term>Glutathion (pharmacologie)</term><term>Lignées consanguines de rats (MeSH)</term><term>Masse moléculaire (MeSH)</term><term>Oxidoreductases (isolement et purification)</term><term>Oxidoreductases (métabolisme)</term><term>Protein-disulfide reductase (glutathione) (MeSH)</term><term>Rats (MeSH)</term><term>Ricine (pharmacologie)</term><term>Techniques in vitro (MeSH)</term><term>Xanthine dehydrogenase (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Oxidoreductases</term><term>Xanthine Dehydrogenase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Disulfides</term><term>Glutathione</term><term>Ricin</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Foie</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Liver</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Oxidoreductases</term><term>Xanthine dehydrogenase</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Disulfures</term><term>Glutathion</term><term>Ricine</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Glutaredoxins</term><term>In Vitro Techniques</term><term>Molecular Weight</term><term>Protein Biosynthesis</term><term>Protein Disulfide Reductase (Glutathione)</term><term>Rats</term><term>Rats, Inbred Strains</term><term>Tissue Distribution</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Biosynthèse des protéines</term><term>Distribution tissulaire</term><term>Glutarédoxines</term><term>Lignées consanguines de rats</term><term>Masse moléculaire</term><term>Protein-disulfide reductase (glutathione)</term><term>Rats</term><term>Techniques in vitro</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A new GSSG-dependent thiol:disulphide oxidoreductase was extensively purified from rat liver cytosol. The enzymic protein shows molecular weight 40 000 as determined by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, and 43 000 as determined by thin-layer gel filtration on Bio-Gel P-100. The pI is 8.1. This enzyme converts rat liver xanthine dehydrogenase into an oxidase, in the presence of oxidized glutathione. Other disulphide compounds are either inactive or far less active than oxidized glutathione in the enzymic oxidation of rat liver xanthine dehydrogenase. The enzyme also catalyses the reduction of the disulphide bond of ricin and acts as a thioltransferase and as a GSH:insulin transhydrogenase. The enzymic activity was measured in various organs of newborn and adult rats.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">6960894</PMID><DateCompleted><Year>1983</Year><Month>02</Month><Day>14</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>01</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0264-6021</ISSN><JournalIssue CitedMedium="Print"><Volume>207</Volume><Issue>1</Issue><PubDate><Year>1982</Year><Month>Oct</Month><Day>01</Day></PubDate></JournalIssue><Title>The Biochemical journal</Title><ISOAbbreviation>Biochem J</ISOAbbreviation></Journal><ArticleTitle>Purification and properties of a new glutathione-dependent thiol:disulphide oxidoreductase from rat liver.</ArticleTitle><Pagination><MedlinePgn>133-8</MedlinePgn></Pagination><Abstract><AbstractText>A new GSSG-dependent thiol:disulphide oxidoreductase was extensively purified from rat liver cytosol. The enzymic protein shows molecular weight 40 000 as determined by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, and 43 000 as determined by thin-layer gel filtration on Bio-Gel P-100. The pI is 8.1. This enzyme converts rat liver xanthine dehydrogenase into an oxidase, in the presence of oxidized glutathione. Other disulphide compounds are either inactive or far less active than oxidized glutathione in the enzymic oxidation of rat liver xanthine dehydrogenase. The enzyme also catalyses the reduction of the disulphide bond of ricin and acts as a thioltransferase and as a GSH:insulin transhydrogenase. The enzymic activity was measured in various organs of newborn and adult rats.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Battelli</LastName><ForeName>M G</ForeName><Initials>MG</Initials></Author><Author ValidYN="Y"><LastName>Lorenzoni</LastName><ForeName>E</ForeName><Initials>E</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Biochem J</MedlineTA><NlmUniqueID>2984726R</NlmUniqueID><ISSNLinking>0264-6021</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004220">Disulfides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>9009-86-3</RegistryNumber><NameOfSubstance UI="D012276">Ricin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.17.1.4</RegistryNumber><NameOfSubstance UI="D014968">Xanthine Dehydrogenase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.4.2</RegistryNumber><NameOfSubstance UI="D011490">Protein Disulfide Reductase (Glutathione)</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D066298" MajorTopicYN="N">In Vitro Techniques</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008099" MajorTopicYN="N">Liver</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008970" MajorTopicYN="N">Molecular Weight</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014176" MajorTopicYN="N">Protein Biosynthesis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011490" MajorTopicYN="Y">Protein Disulfide Reductase (Glutathione)</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051381" MajorTopicYN="N">Rats</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011919" MajorTopicYN="N">Rats, Inbred Strains</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012276" MajorTopicYN="N">Ricin</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014018" MajorTopicYN="N">Tissue Distribution</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014968" MajorTopicYN="N">Xanthine Dehydrogenase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1982</Year><Month>10</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1982</Year><Month>10</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1982</Year><Month>10</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">6960894</ArticleId><ArticleId IdType="pmc">PMC1153833</ArticleId><ArticleId IdType="doi">10.1042/bj2070133</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>J Biol Chem. 1966 Apr 10;241(7):1562-7</Citation><ArticleIdList><ArticleId IdType="pubmed">5946614</ArticleId></ArticleIdList></Reference><Reference><Citation>Lancet. 1968 Apr 20;1(7547):847-8</Citation><ArticleIdList><ArticleId IdType="pubmed">4172401</ArticleId></ArticleIdList></Reference><Reference><Citation>Bull Soc Chim Biol (Paris). 1968 Sep 28;50(5):1023-34</Citation><ArticleIdList><ArticleId IdType="pubmed">5724470</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1969 Jul 25;244(14):3855-63</Citation><ArticleIdList><ArticleId IdType="pubmed">4308738</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1969 Aug 25;244(16):4406-12</Citation><ArticleIdList><ArticleId IdType="pubmed">5806584</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochim Biophys Acta. 1972 May 9;266(2):543-7</Citation><ArticleIdList><ArticleId IdType="pubmed">4338881</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem J. 1972 Feb;126(3):739-45</Citation><ArticleIdList><ArticleId IdType="pubmed">4342395</ArticleId></ArticleIdList></Reference><Reference><Citation>Eur J Biochem. 1973 Jan 3;32(1):27-35</Citation><ArticleIdList><ArticleId IdType="pubmed">4405719</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochim Biophys Acta. 1972 Nov 24;286(1):126-35</Citation><ArticleIdList><ArticleId IdType="pubmed">4633483</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 1973 Jul 31;12(16):3121-6</Citation><ArticleIdList><ArticleId IdType="pubmed">4730499</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 1974 Jan 1;13(1):196-204</Citation><ArticleIdList><ArticleId IdType="pubmed">4202710</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1974 Jan 10;249(1):205-10</Citation><ArticleIdList><ArticleId IdType="pubmed">4809626</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1975 Apr 10;250(7):2532-8</Citation><ArticleIdList><ArticleId IdType="pubmed">1123323</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1975 Jul 25;250(14):5475-80</Citation><ArticleIdList><ArticleId IdType="pubmed">237922</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem J. 1975 Sep;149(3):785-8</Citation><ArticleIdList><ArticleId IdType="pubmed">1201003</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem J. 1976 Nov;159(2):377-84</Citation><ArticleIdList><ArticleId IdType="pubmed">11783</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 1978 Jul 25;17(15):2978-84</Citation><ArticleIdList><ArticleId IdType="pubmed">698179</ArticleId></ArticleIdList></Reference><Reference><Citation>Arch Biochem Biophys. 1978 Aug;189(2):354-63</Citation><ArticleIdList><ArticleId IdType="pubmed">30408</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1979 Sep 25;254(18):9113-9</Citation><ArticleIdList><ArticleId IdType="pubmed">39074</ArticleId></ArticleIdList></Reference><Reference><Citation>Int Rev Cytol. 1978;54:109-60</Citation><ArticleIdList><ArticleId IdType="pubmed">42630</ArticleId></ArticleIdList></Reference><Reference><Citation>FEBS Lett. 1980 Apr 21;113(1):47-51</Citation><ArticleIdList><ArticleId IdType="pubmed">6892902</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochim Biophys Acta. 1980 Oct;615(2):309-23</Citation><ArticleIdList><ArticleId IdType="pubmed">6251889</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochim Biophys Acta. 1980 Jun 13;613(2):324-36</Citation><ArticleIdList><ArticleId IdType="pubmed">6934831</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem J. 1980 Sep 15;190(3):843-5</Citation><ArticleIdList><ArticleId IdType="pubmed">7470084</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem J. 1980 Nov 1;191(2):373-88</Citation><ArticleIdList><ArticleId IdType="pubmed">7236202</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochim Biophys Acta. 1981 Sep 15;661(1):63-73</Citation><ArticleIdList><ArticleId IdType="pubmed">7295733</ArticleId></ArticleIdList></Reference><Reference><Citation>Arch Biochem Biophys. 1981 Oct 1;211(1):44-7</Citation><ArticleIdList><ArticleId IdType="pubmed">6946727</ArticleId></ArticleIdList></Reference><Reference><Citation>J Chromatogr. 1964 Oct;16:167-75</Citation><ArticleIdList><ArticleId IdType="pubmed">14226343</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1962 May;237:1589-95</Citation><ArticleIdList><ArticleId IdType="pubmed">14474846</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1962 Mar;237:760-7</Citation><ArticleIdList><ArticleId IdType="pubmed">13860531</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list></list><tree><noCountry><name sortKey="Battelli, M G" sort="Battelli, M G" uniqKey="Battelli M" first="M G" last="Battelli">M G Battelli</name><name sortKey="Lorenzoni, E" sort="Lorenzoni, E" uniqKey="Lorenzoni E" first="E" last="Lorenzoni">E. Lorenzoni</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/GlutaredoxinV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001368 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 001368 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= GlutaredoxinV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:6960894
|texte= Purification and properties of a new glutathione-dependent thiol:disulphide oxidoreductase from rat liver.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:6960894" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a GlutaredoxinV1
| This area was generated with Dilib version V0.6.37. |  |