Purification and characterization of a glutathione dependent dehydroascorbate reductase from human erythrocytes.
Identifieur interne : 001198 ( Main/Exploration ); précédent : 001197; suivant : 001199Purification and characterization of a glutathione dependent dehydroascorbate reductase from human erythrocytes.
Auteurs : D P Xu [États-Unis] ; M P Washburn ; G P Sun ; W W WellsSource :
- Biochemical and biophysical research communications [ 0006-291X ] ; 1996.
Descripteurs français
- KwdFr :
- Chromatographie d'échange d'ions (MeSH), Cinétique (MeSH), Focalisation isoélectrique (MeSH), Glutarédoxines (MeSH), Glutathion (métabolisme), Humains (MeSH), Oxidoreductases (isolement et purification), Oxidoreductases (sang), Protein-disulfide reductase (glutathione) (MeSH), Électrophorèse sur gel de polyacrylamide (MeSH), Érythrocytes (enzymologie).
- MESH :
- enzymologie : Érythrocytes.
- isolement et purification : Oxidoreductases.
- métabolisme : Glutathion.
- sang : Oxidoreductases.
- Chromatographie d'échange d'ions, Cinétique, Focalisation isoélectrique, Glutarédoxines, Humains, Protein-disulfide reductase (glutathione), Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- Chromatography, Ion Exchange (MeSH), Electrophoresis, Polyacrylamide Gel (MeSH), Erythrocytes (enzymology), Glutaredoxins (MeSH), Glutathione (metabolism), Humans (MeSH), Isoelectric Focusing (MeSH), Kinetics (MeSH), Oxidoreductases (blood), Oxidoreductases (isolation & purification), Protein Disulfide Reductase (Glutathione) (MeSH).
- MESH :
- chemical , blood : Oxidoreductases.
- chemical , isolation & purification : Oxidoreductases.
- chemical , metabolism : Glutathione.
- chemical : Glutaredoxins, Protein Disulfide Reductase (Glutathione).
- enzymology : Erythrocytes.
- Chromatography, Ion Exchange, Electrophoresis, Polyacrylamide Gel, Humans, Isoelectric Focusing, Kinetics.
Abstract
A GSH-dependent dehydroascorbate reductase (EC 1.8.5.1) was purified to homogeneity from human erythrocytes. The enzyme was a monomer of 32 kDa and was purified 133-fold from a crude DEAE-Sepharose fraction with a 25% yield. The reduced protein had a pI of 5.1 as judged by isoelectric focusing. Kinetic analysis gave a Kcat of 316 min-1, a Km of 0.21 mM for DHA with a Kcat/Km of 2.47 x 10(4) M-1 sec-1, and a Km of 3.5 mM for GSH with a Kcat/Km of 1.51 x 10(3) M-1 sec-1. This is the second DHA reductase (after thioltransferase) isolated from human erythrocytes, but unlike thioltransferase, it has no thiol-disulfide oxido-reductase activity.
DOI: 10.1006/bbrc.1996.0555
PubMed: 8660320
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Sun</name></author><author><name sortKey="Wells, W W" sort="Wells, W W" uniqKey="Wells W" first="W W" last="Wells">W W Wells</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1996">1996</date><idno type="RBID">pubmed:8660320</idno><idno type="pmid">8660320</idno><idno type="doi">10.1006/bbrc.1996.0555</idno><idno type="wicri:Area/Main/Corpus">001199</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001199</idno><idno type="wicri:Area/Main/Curation">001199</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001199</idno><idno type="wicri:Area/Main/Exploration">001199</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Purification and characterization of a glutathione dependent dehydroascorbate reductase from human erythrocytes.</title><author><name sortKey="Xu, D P" sort="Xu, D P" uniqKey="Xu D" first="D P" last="Xu">D P Xu</name><affiliation wicri:level="4"><nlm:affiliation>Department of Biochemistry, Michigan State University, Michigan 48824, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry, Michigan State University, Michigan 48824</wicri:regionArea><orgName type="university">Université d'État du Michigan</orgName><placeName><settlement type="city">East Lansing</settlement><region type="state">Michigan</region></placeName></affiliation></author><author><name sortKey="Washburn, M P" sort="Washburn, M P" uniqKey="Washburn M" first="M P" last="Washburn">M P Washburn</name></author><author><name sortKey="Sun, G P" sort="Sun, G P" uniqKey="Sun G" first="G P" last="Sun">G P Sun</name></author><author><name sortKey="Wells, W W" sort="Wells, W W" uniqKey="Wells W" first="W W" last="Wells">W W Wells</name></author></analytic><series><title level="j">Biochemical and biophysical research communications</title><idno type="ISSN">0006-291X</idno><imprint><date when="1996" 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reductase (glutathione) (MeSH)</term><term>Électrophorèse sur gel de polyacrylamide (MeSH)</term><term>Érythrocytes (enzymologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="blood" xml:lang="en"><term>Oxidoreductases</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>Glutathione</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Glutaredoxins</term><term>Protein Disulfide Reductase (Glutathione)</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Érythrocytes</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Erythrocytes</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>Glutathion</term></keywords><keywords scheme="MESH" qualifier="sang" xml:lang="fr"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Chromatography, Ion Exchange</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Humans</term><term>Isoelectric Focusing</term><term>Kinetics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Chromatographie d'échange d'ions</term><term>Cinétique</term><term>Focalisation isoélectrique</term><term>Glutarédoxines</term><term>Humains</term><term>Protein-disulfide reductase (glutathione)</term><term>Électrophorèse sur gel de polyacrylamide</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A GSH-dependent dehydroascorbate reductase (EC 1.8.5.1) was purified to homogeneity from human erythrocytes. The enzyme was a monomer of 32 kDa and was purified 133-fold from a crude DEAE-Sepharose fraction with a 25% yield. The reduced protein had a pI of 5.1 as judged by isoelectric focusing. Kinetic analysis gave a Kcat of 316 min-1, a Km of 0.21 mM for DHA with a Kcat/Km of 2.47 x 10(4) M-1 sec-1, and a Km of 3.5 mM for GSH with a Kcat/Km of 1.51 x 10(3) M-1 sec-1. This is the second DHA reductase (after thioltransferase) isolated from human erythrocytes, but unlike thioltransferase, it has no thiol-disulfide oxido-reductase activity.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8660320</PMID><DateCompleted><Year>1996</Year><Month>07</Month><Day>29</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-291X</ISSN><JournalIssue CitedMedium="Print"><Volume>221</Volume><Issue>1</Issue><PubDate><Year>1996</Year><Month>Apr</Month><Day>05</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation></Journal><ArticleTitle>Purification and characterization of a glutathione dependent dehydroascorbate reductase from human erythrocytes.</ArticleTitle><Pagination><MedlinePgn>117-21</MedlinePgn></Pagination><Abstract><AbstractText>A GSH-dependent dehydroascorbate reductase (EC 1.8.5.1) was purified to homogeneity from human erythrocytes. The enzyme was a monomer of 32 kDa and was purified 133-fold from a crude DEAE-Sepharose fraction with a 25% yield. The reduced protein had a pI of 5.1 as judged by isoelectric focusing. Kinetic analysis gave a Kcat of 316 min-1, a Km of 0.21 mM for DHA with a Kcat/Km of 2.47 x 10(4) M-1 sec-1, and a Km of 3.5 mM for GSH with a Kcat/Km of 1.51 x 10(3) M-1 sec-1. 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States</Country></Grant><Grant><GrantID>DA-44456</GrantID><Acronym>DA</Acronym><Agency>NIDA NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>ES-07255</GrantID><Acronym>ES</Acronym><Agency>NIEHS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochem Biophys Res Commun</MedlineTA><NlmUniqueID>0372516</NlmUniqueID><ISSNLinking>0006-291X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.4.2</RegistryNumber><NameOfSubstance UI="D011490">Protein Disulfide Reductase (Glutathione)</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.5.1</RegistryNumber><NameOfSubstance UI="C020666">glutathione dehydrogenase (ascorbate)</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002852" MajorTopicYN="N">Chromatography, Ion Exchange</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004912" MajorTopicYN="N">Erythrocytes</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007525" MajorTopicYN="N">Isoelectric Focusing</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000097" MajorTopicYN="Y">blood</QualifierName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011490" MajorTopicYN="Y">Protein Disulfide Reductase (Glutathione)</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1996</Year><Month>4</Month><Day>5</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1996</Year><Month>4</Month><Day>5</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1996</Year><Month>4</Month><Day>5</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">8660320</ArticleId><ArticleId IdType="pii">S0006-291X(96)90555-0</ArticleId><ArticleId IdType="doi">10.1006/bbrc.1996.0555</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Michigan</li></region><settlement><li>East Lansing</li></settlement><orgName><li>Université d'État du Michigan</li></orgName></list><tree><noCountry><name sortKey="Sun, G P" sort="Sun, G P" uniqKey="Sun G" first="G P" last="Sun">G P Sun</name><name sortKey="Washburn, M P" sort="Washburn, M P" uniqKey="Washburn M" first="M P" last="Washburn">M P Washburn</name><name sortKey="Wells, W W" sort="Wells, W W" uniqKey="Wells W" first="W W" last="Wells">W W Wells</name></noCountry><country name="États-Unis"><region name="Michigan"><name sortKey="Xu, D P" sort="Xu, D P" uniqKey="Xu D" first="D P" last="Xu">D P Xu</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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