Identification and localization of the first glutaredoxin in leaves of a higher plant.
Identifieur interne : 001222 ( Main/Exploration ); précédent : 001221; suivant : 001223Identification and localization of the first glutaredoxin in leaves of a higher plant.
Auteurs : S. Morell [Allemagne] ; H. Follmann ; I. H BerleinSource :
- FEBS letters [ 0014-5793 ] ; 1995.
Descripteurs français
- KwdFr :
- Antienzymes (métabolisme), Chloroplastes (enzymologie), Données de séquences moléculaires (MeSH), Escherichia coli (composition chimique), Feuilles de plante (enzymologie), Glutarédoxines (MeSH), Inhibiteurs trypsiques (MeSH), Masse moléculaire (MeSH), Oxidoreductases (composition chimique), Oxidoreductases (immunologie), Oxidoreductases (isolement et purification), Oxidoreductases (métabolisme), Protein-disulfide reductase (glutathione) (MeSH), Protéines (immunologie), Protéines (métabolisme), Protéines bactériennes (métabolisme), Protéines végétales (composition chimique), Protéines végétales (immunologie), Protéines végétales (isolement et purification), Protéines végétales (métabolisme), Réactions croisées (MeSH), Spinacia oleracea (enzymologie), Séquence d'acides aminés (MeSH), alpha-Amylases (antagonistes et inhibiteurs).
- MESH :
- antagonistes et inhibiteurs : alpha-Amylases.
- composition chimique : Escherichia coli, Oxidoreductases, Protéines végétales.
- enzymologie : Chloroplastes, Feuilles de plante, Spinacia oleracea.
- immunologie : Oxidoreductases, Protéines, Protéines végétales.
- isolement et purification : Oxidoreductases, Protéines végétales.
- métabolisme : Antienzymes, Oxidoreductases, Protéines, Protéines bactériennes, Protéines végétales.
- Données de séquences moléculaires, Glutarédoxines, Inhibiteurs trypsiques, Masse moléculaire, Protein-disulfide reductase (glutathione), Réactions croisées, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Bacterial Proteins (metabolism), Chloroplasts (enzymology), Cross Reactions (MeSH), Enzyme Inhibitors (metabolism), Escherichia coli (chemistry), Glutaredoxins (MeSH), Molecular Sequence Data (MeSH), Molecular Weight (MeSH), Oxidoreductases (chemistry), Oxidoreductases (immunology), Oxidoreductases (isolation & purification), Oxidoreductases (metabolism), Plant Leaves (enzymology), Plant Proteins (chemistry), Plant Proteins (immunology), Plant Proteins (isolation & purification), Plant Proteins (metabolism), Protein Disulfide Reductase (Glutathione) (MeSH), Proteins (immunology), Proteins (metabolism), Spinacia oleracea (enzymology), Trypsin Inhibitors (MeSH), alpha-Amylases (antagonists & inhibitors).
- MESH :
- chemical , antagonists & inhibitors : alpha-Amylases.
- chemical , chemistry : Oxidoreductases, Plant Proteins.
- chemical , immunology : Oxidoreductases, Plant Proteins, Proteins.
- chemical , isolation & purification : Oxidoreductases, Plant Proteins.
- chemical , metabolism : Bacterial Proteins, Enzyme Inhibitors, Oxidoreductases, Plant Proteins, Proteins.
- chemistry : Escherichia coli.
- enzymology : Chloroplasts, Plant Leaves, Spinacia oleracea.
- Amino Acid Sequence, Cross Reactions, Glutaredoxins, Molecular Sequence Data, Molecular Weight, Protein Disulfide Reductase (Glutathione), Trypsin Inhibitors.
Abstract
Glutaredoxin(thioltransferase) has been identified and purified to homogeneity from spinach leaves. Its cytosolic localization was demonstrated by chromatographic and immunological analysis of extracts from isolated spinach chloroplasts and mitochondria, respectively. Spinach glutaredoxin shows a significant crossreactivity with antibodies raised against E. coli glutaredoxin and possesses a specific thioltransferase activity comparable to that of the E. coli protein. Minor thioltransferase activities (less than 10% of total leaf activity) have been observed in spinach chloroplasts which are probably due to the presence of trypsin inhibitor and thioredoxins (TRf and TRm).
DOI: 10.1016/0014-5793(95)00690-b
PubMed: 7649248
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Morell</name><affiliation wicri:level="1"><nlm:affiliation>University of Kassel, Department of Biochemistry, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>University of Kassel, Department of Biochemistry</wicri:regionArea><wicri:noRegion>Department of Biochemistry</wicri:noRegion><wicri:noRegion>Department of Biochemistry</wicri:noRegion><wicri:noRegion>Department of Biochemistry</wicri:noRegion></affiliation></author><author><name sortKey="Follmann, H" sort="Follmann, H" uniqKey="Follmann H" first="H" last="Follmann">H. Follmann</name></author><author><name sortKey="H Berlein, I" sort="H Berlein, I" uniqKey="H Berlein I" first="I" last="H Berlein">I. 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(métabolisme)</term><term>Protéines bactériennes (métabolisme)</term><term>Protéines végétales (composition chimique)</term><term>Protéines végétales (immunologie)</term><term>Protéines végétales (isolement et purification)</term><term>Protéines végétales (métabolisme)</term><term>Réactions croisées (MeSH)</term><term>Spinacia oleracea (enzymologie)</term><term>Séquence d'acides aminés (MeSH)</term><term>alpha-Amylases (antagonistes et inhibiteurs)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>alpha-Amylases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Oxidoreductases</term><term>Plant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Oxidoreductases</term><term>Plant Proteins</term><term>Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" 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moléculaire</term><term>Protein-disulfide reductase (glutathione)</term><term>Réactions croisées</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutaredoxin(thioltransferase) has been identified and purified to homogeneity from spinach leaves. Its cytosolic localization was demonstrated by chromatographic and immunological analysis of extracts from isolated spinach chloroplasts and mitochondria, respectively. Spinach glutaredoxin shows a significant crossreactivity with antibodies raised against E. coli glutaredoxin and possesses a specific thioltransferase activity comparable to that of the E. coli protein. Minor thioltransferase activities (less than 10% of total leaf activity) have been observed in spinach chloroplasts which are probably due to the presence of trypsin inhibitor and thioredoxins (TRf and TRm).</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">7649248</PMID><DateCompleted><Year>1995</Year><Month>09</Month><Day>22</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0014-5793</ISSN><JournalIssue CitedMedium="Print"><Volume>369</Volume><Issue>2-3</Issue><PubDate><Year>1995</Year><Month>Aug</Month><Day>07</Day></PubDate></JournalIssue><Title>FEBS letters</Title><ISOAbbreviation>FEBS Lett</ISOAbbreviation></Journal><ArticleTitle>Identification and localization of the first glutaredoxin in leaves of a higher plant.</ArticleTitle><Pagination><MedlinePgn>149-52</MedlinePgn></Pagination><Abstract><AbstractText>Glutaredoxin(thioltransferase) has been identified and purified to homogeneity from spinach leaves. Its cytosolic localization was demonstrated by chromatographic and immunological analysis of extracts from isolated spinach chloroplasts and mitochondria, respectively. Spinach glutaredoxin shows a significant crossreactivity with antibodies raised against E. coli glutaredoxin and possesses a specific thioltransferase activity comparable to that of the E. coli protein. Minor thioltransferase activities (less than 10% of total leaf activity) have been observed in spinach chloroplasts which are probably due to the presence of trypsin inhibitor and thioredoxins (TRf and TRm).</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Morell</LastName><ForeName>S</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>University of Kassel, Department of Biochemistry, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Follmann</LastName><ForeName>H</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Häberlein</LastName><ForeName>I</ForeName><Initials>I</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>FEBS Lett</MedlineTA><NlmUniqueID>0155157</NlmUniqueID><ISSNLinking>0014-5793</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004791">Enzyme Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014361">Trypsin Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 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UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008970" MajorTopicYN="N">Molecular Weight</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018515" MajorTopicYN="N">Plant Leaves</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011490" MajorTopicYN="Y">Protein Disulfide Reductase (Glutathione)</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018724" MajorTopicYN="N">Spinacia oleracea</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014361" MajorTopicYN="N">Trypsin Inhibitors</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000516" MajorTopicYN="N">alpha-Amylases</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1995</Year><Month>8</Month><Day>7</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1995</Year><Month>8</Month><Day>7</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1995</Year><Month>8</Month><Day>7</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">7649248</ArticleId><ArticleId IdType="pii">0014-5793(95)00690-B</ArticleId><ArticleId IdType="doi">10.1016/0014-5793(95)00690-b</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country></list><tree><noCountry><name sortKey="Follmann, H" sort="Follmann, H" uniqKey="Follmann H" first="H" last="Follmann">H. Follmann</name><name sortKey="H Berlein, I" sort="H Berlein, I" uniqKey="H Berlein I" first="I" last="H Berlein">I. H Berlein</name></noCountry><country name="Allemagne"><noRegion><name sortKey="Morell, S" sort="Morell, S" uniqKey="Morell S" first="S" last="Morell">S. Morell</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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