Purification, cloning and characterization of a novel peroxidase isozyme from sweetpotatoes (Ipomoea batatas).
Identifieur interne : 003A88 ( Main/Exploration ); précédent : 003A87; suivant : 003A89Purification, cloning and characterization of a novel peroxidase isozyme from sweetpotatoes (Ipomoea batatas).
Auteurs : Annette Rompel [Allemagne] ; Michael Albers ; Joseph I. Naseri ; Carsten Gerdemann ; Klaudia Büldt-Karentzopoulos ; Beate Jasper ; Bernt KrebsSource :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2007.
Descripteurs français
- KwdFr :
- Clonage moléculaire (MeSH), Données de séquences moléculaires (MeSH), Ipomoea batatas (enzymologie), Ipomoea batatas (génétique), Isoenzymes (composition chimique), Isoenzymes (génétique), Isoenzymes (isolement et purification), Myeloperoxidase (composition chimique), Myeloperoxidase (génétique), Myeloperoxidase (isolement et purification), Similitude de séquences (MeSH), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH).
- MESH :
- composition chimique : Isoenzymes, Myeloperoxidase.
- enzymologie : Ipomoea batatas.
- génétique : Ipomoea batatas, Isoenzymes, Myeloperoxidase.
- isolement et purification : Isoenzymes, Myeloperoxidase.
- Clonage moléculaire, Données de séquences moléculaires, Similitude de séquences, Séquence d'acides aminés, Séquence nucléotidique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Base Sequence (MeSH), Cloning, Molecular (MeSH), Ipomoea batatas (enzymology), Ipomoea batatas (genetics), Isoenzymes (chemistry), Isoenzymes (genetics), Isoenzymes (isolation & purification), Molecular Sequence Data (MeSH), Peroxidase (chemistry), Peroxidase (genetics), Peroxidase (isolation & purification), Sequence Homology (MeSH).
- MESH :
- chemical , chemistry : Isoenzymes, Peroxidase.
- enzymology : Ipomoea batatas.
- genetics : Ipomoea batatas, Isoenzymes, Peroxidase.
- chemical , isolation & purification : Isoenzymes, Peroxidase.
- Amino Acid Sequence, Base Sequence, Cloning, Molecular, Molecular Sequence Data, Sequence Homology.
Abstract
An anionic peroxidase from sweetpotato tubers is purified and characterized. The isozyme ibPrx15 is purified to homogeneity by affinity chromatography using a concanavalin A column. The isoelectric point was determined to pI 4.9. MALDI-MS detected a singly charged molecule with a mass of 42029 Da. Absorption spectra of ibPrx15 compounds I, II and III were obtained after treatment with H(2)O(2) at room temperature. Comparative data of ibPrx15 on substrate specificity to tobacco anionic peroxidase (TOP) and horseradish peroxidase (HRP) reveal similar specific activity towards a series of conventional substrates except for iodide, which is a two-electron donor interacting directly with the compound I derivative in the catalytic cycle. ibPrx15 exhibits a high specific activity towards iodide about 10(3)-fold to that of tobacco peroxidase. The amino acid sequence of the main isozyme ibPrx15 was determined by Edman degradation and by sequencing the amplified cDNA fragments. ibPrx15 has 86% identity to another Ipomoea sequence ibPrx05 and 72% identity with a sequence from Populus trichocarpa (PtPrx72).
DOI: 10.1016/j.bbapap.2007.08.013
PubMed: 17936696
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Naseri</name></author><author><name sortKey="Gerdemann, Carsten" sort="Gerdemann, Carsten" uniqKey="Gerdemann C" first="Carsten" last="Gerdemann">Carsten Gerdemann</name></author><author><name sortKey="Buldt Karentzopoulos, Klaudia" sort="Buldt Karentzopoulos, Klaudia" uniqKey="Buldt Karentzopoulos K" first="Klaudia" last="Büldt-Karentzopoulos">Klaudia Büldt-Karentzopoulos</name></author><author><name sortKey="Jasper, Beate" sort="Jasper, Beate" uniqKey="Jasper B" first="Beate" last="Jasper">Beate Jasper</name></author><author><name sortKey="Krebs, Bernt" sort="Krebs, Bernt" uniqKey="Krebs B" first="Bernt" last="Krebs">Bernt Krebs</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2007">2007</date><idno type="RBID">pubmed:17936696</idno><idno type="pmid">17936696</idno><idno type="doi">10.1016/j.bbapap.2007.08.013</idno><idno type="wicri:Area/Main/Corpus">003A48</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">003A48</idno><idno type="wicri:Area/Main/Curation">003A48</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">003A48</idno><idno type="wicri:Area/Main/Exploration">003A48</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Purification, cloning and characterization of a novel peroxidase isozyme from sweetpotatoes (Ipomoea batatas).</title><author><name sortKey="Rompel, Annette" sort="Rompel, Annette" uniqKey="Rompel A" first="Annette" last="Rompel">Annette Rompel</name><affiliation wicri:level="3"><nlm:affiliation>Institut für Biochemie, Westfälische Wilhelms-Universität, Wilhelm-Klemm-Strasse 2, D-48149 Münster, Germany. romela@uni-muenster.de</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institut für Biochemie, Westfälische Wilhelms-Universität, Wilhelm-Klemm-Strasse 2, D-48149 Münster</wicri:regionArea><placeName><region type="land" nuts="1">Rhénanie-du-Nord-Westphalie</region><region type="district" nuts="2">District de Münster</region><settlement type="city">Münster</settlement></placeName></affiliation></author><author><name sortKey="Albers, Michael" sort="Albers, Michael" uniqKey="Albers M" first="Michael" last="Albers">Michael Albers</name></author><author><name sortKey="Naseri, Joseph I" sort="Naseri, Joseph I" uniqKey="Naseri J" first="Joseph I" last="Naseri">Joseph I. Naseri</name></author><author><name sortKey="Gerdemann, Carsten" sort="Gerdemann, Carsten" uniqKey="Gerdemann C" first="Carsten" last="Gerdemann">Carsten Gerdemann</name></author><author><name sortKey="Buldt Karentzopoulos, Klaudia" sort="Buldt Karentzopoulos, Klaudia" uniqKey="Buldt Karentzopoulos K" first="Klaudia" last="Büldt-Karentzopoulos">Klaudia Büldt-Karentzopoulos</name></author><author><name sortKey="Jasper, Beate" sort="Jasper, Beate" uniqKey="Jasper B" first="Beate" last="Jasper">Beate Jasper</name></author><author><name sortKey="Krebs, Bernt" sort="Krebs, Bernt" uniqKey="Krebs B" first="Bernt" last="Krebs">Bernt Krebs</name></author></analytic><series><title level="j">Biochimica et biophysica acta</title><idno type="ISSN">0006-3002</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Base Sequence (MeSH)</term><term>Cloning, Molecular (MeSH)</term><term>Ipomoea batatas (enzymology)</term><term>Ipomoea batatas (genetics)</term><term>Isoenzymes (chemistry)</term><term>Isoenzymes (genetics)</term><term>Isoenzymes (isolation & purification)</term><term>Molecular Sequence Data (MeSH)</term><term>Peroxidase (chemistry)</term><term>Peroxidase (genetics)</term><term>Peroxidase (isolation & purification)</term><term>Sequence Homology (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Clonage moléculaire (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Ipomoea batatas (enzymologie)</term><term>Ipomoea batatas (génétique)</term><term>Isoenzymes (composition chimique)</term><term>Isoenzymes (génétique)</term><term>Isoenzymes (isolement et purification)</term><term>Myeloperoxidase (composition chimique)</term><term>Myeloperoxidase (génétique)</term><term>Myeloperoxidase (isolement et purification)</term><term>Similitude de séquences (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Séquence nucléotidique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Isoenzymes</term><term>Peroxidase</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Isoenzymes</term><term>Myeloperoxidase</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Ipomoea batatas</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Ipomoea batatas</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Ipomoea batatas</term><term>Isoenzymes</term><term>Peroxidase</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Ipomoea batatas</term><term>Isoenzymes</term><term>Myeloperoxidase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Isoenzymes</term><term>Peroxidase</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Isoenzymes</term><term>Myeloperoxidase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Base Sequence</term><term>Cloning, Molecular</term><term>Molecular Sequence Data</term><term>Sequence Homology</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Clonage moléculaire</term><term>Données de séquences moléculaires</term><term>Similitude de séquences</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">An anionic peroxidase from sweetpotato tubers is purified and characterized. The isozyme ibPrx15 is purified to homogeneity by affinity chromatography using a concanavalin A column. The isoelectric point was determined to pI 4.9. MALDI-MS detected a singly charged molecule with a mass of 42029 Da. Absorption spectra of ibPrx15 compounds I, II and III were obtained after treatment with H(2)O(2) at room temperature. Comparative data of ibPrx15 on substrate specificity to tobacco anionic peroxidase (TOP) and horseradish peroxidase (HRP) reveal similar specific activity towards a series of conventional substrates except for iodide, which is a two-electron donor interacting directly with the compound I derivative in the catalytic cycle. ibPrx15 exhibits a high specific activity towards iodide about 10(3)-fold to that of tobacco peroxidase. The amino acid sequence of the main isozyme ibPrx15 was determined by Edman degradation and by sequencing the amplified cDNA fragments. ibPrx15 has 86% identity to another Ipomoea sequence ibPrx05 and 72% identity with a sequence from Populus trichocarpa (PtPrx72).</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17936696</PMID><DateCompleted><Year>2008</Year><Month>01</Month><Day>24</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>26</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0006-3002</ISSN><JournalIssue CitedMedium="Print"><Volume>1774</Volume><Issue>11</Issue><PubDate><Year>2007</Year><Month>Nov</Month></PubDate></JournalIssue><Title>Biochimica et biophysica acta</Title><ISOAbbreviation>Biochim Biophys Acta</ISOAbbreviation></Journal><ArticleTitle>Purification, cloning and characterization of a novel peroxidase isozyme from sweetpotatoes (Ipomoea batatas).</ArticleTitle><Pagination><MedlinePgn>1422-30</MedlinePgn></Pagination><Abstract><AbstractText>An anionic peroxidase from sweetpotato tubers is purified and characterized. The isozyme ibPrx15 is purified to homogeneity by affinity chromatography using a concanavalin A column. The isoelectric point was determined to pI 4.9. MALDI-MS detected a singly charged molecule with a mass of 42029 Da. Absorption spectra of ibPrx15 compounds I, II and III were obtained after treatment with H(2)O(2) at room temperature. Comparative data of ibPrx15 on substrate specificity to tobacco anionic peroxidase (TOP) and horseradish peroxidase (HRP) reveal similar specific activity towards a series of conventional substrates except for iodide, which is a two-electron donor interacting directly with the compound I derivative in the catalytic cycle. ibPrx15 exhibits a high specific activity towards iodide about 10(3)-fold to that of tobacco peroxidase. The amino acid sequence of the main isozyme ibPrx15 was determined by Edman degradation and by sequencing the amplified cDNA fragments. ibPrx15 has 86% identity to another Ipomoea sequence ibPrx05 and 72% identity with a sequence from Populus trichocarpa (PtPrx72).</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rompel</LastName><ForeName>Annette</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Institut für Biochemie, Westfälische Wilhelms-Universität, Wilhelm-Klemm-Strasse 2, D-48149 Münster, Germany. romela@uni-muenster.de</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Albers</LastName><ForeName>Michael</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Naseri</LastName><ForeName>Joseph I</ForeName><Initials>JI</Initials></Author><Author ValidYN="Y"><LastName>Gerdemann</LastName><ForeName>Carsten</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Büldt-Karentzopoulos</LastName><ForeName>Klaudia</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Jasper</LastName><ForeName>Beate</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Krebs</LastName><ForeName>Bernt</ForeName><Initials>B</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>GENBANK</DataBankName><AccessionNumberList><AccessionNumber>AJ242742</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2007</Year><Month>08</Month><Day>28</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta</MedlineTA><NlmUniqueID>0217513</NlmUniqueID><ISSNLinking>0006-3002</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007527">Isoenzymes</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.7</RegistryNumber><NameOfSubstance UI="D009195">Peroxidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D027723" MajorTopicYN="N">Ipomoea batatas</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007527" MajorTopicYN="N">Isoenzymes</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009195" MajorTopicYN="N">Peroxidase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017385" MajorTopicYN="N">Sequence Homology</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2006</Year><Month>11</Month><Day>24</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2007</Year><Month>08</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2007</Year><Month>08</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>10</Month><Day>16</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2008</Year><Month>1</Month><Day>25</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>10</Month><Day>16</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17936696</ArticleId><ArticleId IdType="pii">S1570-9639(07)00201-4</ArticleId><ArticleId IdType="doi">10.1016/j.bbapap.2007.08.013</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country><region><li>District de Münster</li><li>Rhénanie-du-Nord-Westphalie</li></region><settlement><li>Münster</li></settlement></list><tree><noCountry><name sortKey="Albers, Michael" sort="Albers, Michael" uniqKey="Albers M" first="Michael" last="Albers">Michael Albers</name><name sortKey="Buldt Karentzopoulos, Klaudia" sort="Buldt Karentzopoulos, Klaudia" uniqKey="Buldt Karentzopoulos K" first="Klaudia" last="Büldt-Karentzopoulos">Klaudia Büldt-Karentzopoulos</name><name sortKey="Gerdemann, Carsten" sort="Gerdemann, Carsten" uniqKey="Gerdemann C" first="Carsten" last="Gerdemann">Carsten Gerdemann</name><name sortKey="Jasper, Beate" sort="Jasper, Beate" uniqKey="Jasper B" first="Beate" last="Jasper">Beate Jasper</name><name sortKey="Krebs, Bernt" sort="Krebs, Bernt" uniqKey="Krebs B" first="Bernt" last="Krebs">Bernt Krebs</name><name sortKey="Naseri, Joseph I" sort="Naseri, Joseph I" uniqKey="Naseri J" first="Joseph I" last="Naseri">Joseph I. Naseri</name></noCountry><country name="Allemagne"><region name="Rhénanie-du-Nord-Westphalie"><name sortKey="Rompel, Annette" sort="Rompel, Annette" uniqKey="Rompel A" first="Annette" last="Rompel">Annette Rompel</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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