Role of the NADP/thioredoxin system in the reduction of alpha-amylase and trypsin inhibitor proteins.
Identifieur interne : 001296 ( Main/Exploration ); précédent : 001295; suivant : 001297Role of the NADP/thioredoxin system in the reduction of alpha-amylase and trypsin inhibitor proteins.
Auteurs : K. Kobrehel ; B C Yee ; B B BuchananSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 1991.
Descripteurs français
- KwdFr :
- Activation enzymatique (MeSH), Colorants fluorescents (MeSH), Escherichia coli (métabolisme), Inhibiteurs trypsiques (métabolisme), Malate dehydrogenase (NADP+) (MeSH), Malate dehydrogenase (métabolisme), NADP (métabolisme), Oxydoréduction (MeSH), Thiorédoxines (métabolisme), alpha-Amylases (antagonistes et inhibiteurs), alpha-Amylases (métabolisme), Électrophorèse sur gel de polyacrylamide (MeSH).
- MESH :
- antagonistes et inhibiteurs : alpha-Amylases.
- métabolisme : Escherichia coli, Inhibiteurs trypsiques, Malate dehydrogenase, NADP, Thiorédoxines, alpha-Amylases.
- Activation enzymatique, Colorants fluorescents, Malate dehydrogenase (NADP+), Oxydoréduction, Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- Electrophoresis, Polyacrylamide Gel (MeSH), Enzyme Activation (MeSH), Escherichia coli (metabolism), Fluorescent Dyes (MeSH), Malate Dehydrogenase (NADP+) (MeSH), Malate Dehydrogenase (metabolism), NADP (metabolism), Oxidation-Reduction (MeSH), Thioredoxins (metabolism), Trypsin Inhibitors (metabolism), alpha-Amylases (antagonists & inhibitors), alpha-Amylases (metabolism).
- MESH :
- chemical , antagonists & inhibitors : alpha-Amylases.
- chemical , metabolism : Malate Dehydrogenase, NADP, Thioredoxins, Trypsin Inhibitors, alpha-Amylases.
- chemical : Fluorescent Dyes, Malate Dehydrogenase (NADP+).
- metabolism : Escherichia coli.
- Electrophoresis, Polyacrylamide Gel, Enzyme Activation, Oxidation-Reduction.
Abstract
Thioredoxin, reduced either enzymatically with NADPH and NADP-thioredoxin reductase or chemically with dithiothreitol, reduced alpha-amylase and trypsin inhibitor proteins from several sources. Included were cystine-rich seed representatives from wheat (alpha-amylase inhibitors), soybean (Bowman-Birk trypsin inhibitor), and corn (kernel trypsin inhibitor). This system also reduced other trypsin inhibitors: the soybean Kunitz inhibitor, bovine lung aprotinin, and egg white ovoinhibitor and ovomucoid proteins. The ability of these proteins to undergo reduction by thioredoxin was determined by 1) a coupled enzyme activation assay with chloroplast NADP-malate dehydrogenase or fructose-1,6-bisphosphatase, 2) a dye reduction assay with 5',5'-dithiobis(2-nitrobenzoic acid), and 3) a direct reduction method based on the fluorescent probe, monobromobimane, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Reduction experiments with the seed proteins were carried out with thioredoxin from wheat germ (h-type) or Escherichia coli; the corresponding experiments with the animal trypsin inhibitors were carried out with thioredoxin from calf thymus or E. coli. In all cases, thioredoxin appeared to act catalytically; the reduced form of glutathione was without effect. When considered in conjunction with earlier results on purothionin (confirmed and extended in the current study), the new findings suggest that the NADP/thioredoxin system functions in the reduction of protein inhibitors of seeds and animal tissues. These results also raise the question of the occurrence of glutaredoxin in plants, as E. coli glutaredoxin was found to promote the reduction of some but not all of the proteins tested.
PubMed: 1874751
Affiliations:
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Le document en format XML
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Kobrehel</name><affiliation><nlm:affiliation>Department of Plant Biology, University of California, Berkeley 94720.</nlm:affiliation><wicri:noCountry code="subField">Berkeley 94720</wicri:noCountry></affiliation></author><author><name sortKey="Yee, B C" sort="Yee, B C" uniqKey="Yee B" first="B C" last="Yee">B C Yee</name></author><author><name sortKey="Buchanan, B B" sort="Buchanan, B B" uniqKey="Buchanan B" first="B B" last="Buchanan">B B Buchanan</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1991">1991</date><idno type="RBID">pubmed:1874751</idno><idno type="pmid">1874751</idno><idno type="wicri:Area/Main/Corpus">001295</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001295</idno><idno type="wicri:Area/Main/Curation">001295</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001295</idno><idno type="wicri:Area/Main/Exploration">001295</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Role of the NADP/thioredoxin system in the reduction of alpha-amylase and trypsin inhibitor proteins.</title><author><name sortKey="Kobrehel, K" sort="Kobrehel, K" uniqKey="Kobrehel K" first="K" last="Kobrehel">K. Kobrehel</name><affiliation><nlm:affiliation>Department of Plant Biology, University of California, Berkeley 94720.</nlm:affiliation><wicri:noCountry code="subField">Berkeley 94720</wicri:noCountry></affiliation></author><author><name sortKey="Yee, B C" sort="Yee, B C" uniqKey="Yee B" first="B C" last="Yee">B C Yee</name></author><author><name sortKey="Buchanan, B B" sort="Buchanan, B B" uniqKey="Buchanan B" first="B B" last="Buchanan">B B Buchanan</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="1991" type="published">1991</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Electrophoresis, Polyacrylamide Gel (MeSH)</term><term>Enzyme Activation (MeSH)</term><term>Escherichia coli (metabolism)</term><term>Fluorescent Dyes (MeSH)</term><term>Malate Dehydrogenase (NADP+) (MeSH)</term><term>Malate Dehydrogenase (metabolism)</term><term>NADP (metabolism)</term><term>Oxidation-Reduction (MeSH)</term><term>Thioredoxins (metabolism)</term><term>Trypsin Inhibitors (metabolism)</term><term>alpha-Amylases (antagonists & inhibitors)</term><term>alpha-Amylases (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Activation enzymatique (MeSH)</term><term>Colorants fluorescents (MeSH)</term><term>Escherichia coli (métabolisme)</term><term>Inhibiteurs trypsiques (métabolisme)</term><term>Malate dehydrogenase (NADP+) (MeSH)</term><term>Malate dehydrogenase (métabolisme)</term><term>NADP (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Thiorédoxines (métabolisme)</term><term>alpha-Amylases (antagonistes et inhibiteurs)</term><term>alpha-Amylases (métabolisme)</term><term>Électrophorèse sur gel de polyacrylamide (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>alpha-Amylases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Malate Dehydrogenase</term><term>NADP</term><term>Thioredoxins</term><term>Trypsin Inhibitors</term><term>alpha-Amylases</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Fluorescent Dyes</term><term>Malate Dehydrogenase (NADP+)</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>alpha-Amylases</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Escherichia coli</term><term>Inhibiteurs trypsiques</term><term>Malate dehydrogenase</term><term>NADP</term><term>Thiorédoxines</term><term>alpha-Amylases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Electrophoresis, Polyacrylamide Gel</term><term>Enzyme Activation</term><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Activation enzymatique</term><term>Colorants fluorescents</term><term>Malate dehydrogenase (NADP+)</term><term>Oxydoréduction</term><term>Électrophorèse sur gel de polyacrylamide</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Thioredoxin, reduced either enzymatically with NADPH and NADP-thioredoxin reductase or chemically with dithiothreitol, reduced alpha-amylase and trypsin inhibitor proteins from several sources. Included were cystine-rich seed representatives from wheat (alpha-amylase inhibitors), soybean (Bowman-Birk trypsin inhibitor), and corn (kernel trypsin inhibitor). This system also reduced other trypsin inhibitors: the soybean Kunitz inhibitor, bovine lung aprotinin, and egg white ovoinhibitor and ovomucoid proteins. The ability of these proteins to undergo reduction by thioredoxin was determined by 1) a coupled enzyme activation assay with chloroplast NADP-malate dehydrogenase or fructose-1,6-bisphosphatase, 2) a dye reduction assay with 5',5'-dithiobis(2-nitrobenzoic acid), and 3) a direct reduction method based on the fluorescent probe, monobromobimane, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Reduction experiments with the seed proteins were carried out with thioredoxin from wheat germ (h-type) or Escherichia coli; the corresponding experiments with the animal trypsin inhibitors were carried out with thioredoxin from calf thymus or E. coli. In all cases, thioredoxin appeared to act catalytically; the reduced form of glutathione was without effect. When considered in conjunction with earlier results on purothionin (confirmed and extended in the current study), the new findings suggest that the NADP/thioredoxin system functions in the reduction of protein inhibitors of seeds and animal tissues. These results also raise the question of the occurrence of glutaredoxin in plants, as E. coli glutaredoxin was found to promote the reduction of some but not all of the proteins tested.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">1874751</PMID><DateCompleted><Year>1991</Year><Month>09</Month><Day>26</Day></DateCompleted><DateRevised><Year>2008</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>266</Volume><Issue>24</Issue><PubDate><Year>1991</Year><Month>Aug</Month><Day>25</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Role of the NADP/thioredoxin system in the reduction of alpha-amylase and trypsin inhibitor proteins.</ArticleTitle><Pagination><MedlinePgn>16135-40</MedlinePgn></Pagination><Abstract><AbstractText>Thioredoxin, reduced either enzymatically with NADPH and NADP-thioredoxin reductase or chemically with dithiothreitol, reduced alpha-amylase and trypsin inhibitor proteins from several sources. Included were cystine-rich seed representatives from wheat (alpha-amylase inhibitors), soybean (Bowman-Birk trypsin inhibitor), and corn (kernel trypsin inhibitor). This system also reduced other trypsin inhibitors: the soybean Kunitz inhibitor, bovine lung aprotinin, and egg white ovoinhibitor and ovomucoid proteins. The ability of these proteins to undergo reduction by thioredoxin was determined by 1) a coupled enzyme activation assay with chloroplast NADP-malate dehydrogenase or fructose-1,6-bisphosphatase, 2) a dye reduction assay with 5',5'-dithiobis(2-nitrobenzoic acid), and 3) a direct reduction method based on the fluorescent probe, monobromobimane, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Reduction experiments with the seed proteins were carried out with thioredoxin from wheat germ (h-type) or Escherichia coli; the corresponding experiments with the animal trypsin inhibitors were carried out with thioredoxin from calf thymus or E. coli. In all cases, thioredoxin appeared to act catalytically; the reduced form of glutathione was without effect. When considered in conjunction with earlier results on purothionin (confirmed and extended in the current study), the new findings suggest that the NADP/thioredoxin system functions in the reduction of protein inhibitors of seeds and animal tissues. These results also raise the question of the occurrence of glutaredoxin in plants, as E. coli glutaredoxin was found to promote the reduction of some but not all of the proteins tested.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kobrehel</LastName><ForeName>K</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Plant Biology, University of California, Berkeley 94720.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yee</LastName><ForeName>B C</ForeName><Initials>BC</Initials></Author><Author ValidYN="Y"><LastName>Buchanan</LastName><ForeName>B B</ForeName><Initials>BB</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005456">Fluorescent Dyes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014361">Trypsin Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>53-59-8</RegistryNumber><NameOfSubstance UI="D009249">NADP</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.1.37</RegistryNumber><NameOfSubstance UI="D008291">Malate Dehydrogenase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.1.82</RegistryNumber><NameOfSubstance UI="D050538">Malate Dehydrogenase (NADP+)</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.1</RegistryNumber><NameOfSubstance UI="D000516">alpha-Amylases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CitationSubset>S</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004789" MajorTopicYN="N">Enzyme Activation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005456" MajorTopicYN="N">Fluorescent Dyes</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008291" MajorTopicYN="N">Malate Dehydrogenase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D050538" MajorTopicYN="N">Malate Dehydrogenase (NADP+)</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009249" MajorTopicYN="N">NADP</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014361" MajorTopicYN="N">Trypsin Inhibitors</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000516" MajorTopicYN="N">alpha-Amylases</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><OtherID Source="NASA">91340766</OtherID></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1991</Year><Month>8</Month><Day>25</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1991</Year><Month>8</Month><Day>25</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1991</Year><Month>8</Month><Day>25</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">1874751</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list></list><tree><noCountry><name sortKey="Buchanan, B B" sort="Buchanan, B B" uniqKey="Buchanan B" first="B B" last="Buchanan">B B Buchanan</name><name sortKey="Kobrehel, K" sort="Kobrehel, K" uniqKey="Kobrehel K" first="K" last="Kobrehel">K. 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