Separation of manganese peroxidase isoenzymes on strong anion-exchange monolithic column using pH-salt gradient.
Identifieur interne : 000921 ( Main/Corpus ); précédent : 000920; suivant : 000922Separation of manganese peroxidase isoenzymes on strong anion-exchange monolithic column using pH-salt gradient.
Auteurs : Helena Podgornik ; Ales PodgornikSource :
- Journal of chromatography. B, Analytical technologies in the biomedical and life sciences [ 1570-0232 ] ; 2004.
English descriptors
- KwdEn :
- Anion Exchange Resins (MeSH), Chromatography, High Pressure Liquid (instrumentation), Chromatography, High Pressure Liquid (methods), Hydrogen-Ion Concentration (MeSH), Isoelectric Focusing (MeSH), Isoenzymes (isolation & purification), Peroxidases (isolation & purification), Phanerochaete (enzymology), Salts (chemistry).
- MESH :
- chemical , chemistry : Salts.
- chemical , isolation & purification : Isoenzymes, Peroxidases.
- chemical : Anion Exchange Resins.
- enzymology : Phanerochaete.
- instrumentation : Chromatography, High Pressure Liquid.
- methods : Chromatography, High Pressure Liquid.
- Hydrogen-Ion Concentration, Isoelectric Focusing.
Abstract
Different chromatographic methods including chromatofocusing are used for separation of manganese peroxidase (MnP) isoforms and their isolation from the fungal growth medium. We tested strong anion exchange methacrylate based monolithic columns as a stationary phase for fast separation of MnP's. Sodium acetate buffers of two different pH values (6 and 4) were used for formation of reproducible pH gradient. The entire cycle, involving analysis and column regeneration, was completed in 3 min. Use of pH gradient showed better MnP isoform separation comparing to the salt gradient, while application of combined pH-salt gradient, resulted in further improvement.
DOI: 10.1016/j.jchromb.2003.10.059
PubMed: 14670754
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pubmed:14670754Le document en format XML
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B, Analytical technologies in the biomedical and life sciences</title><idno type="ISSN">1570-0232</idno><imprint><date when="2004" type="published">2004</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Anion Exchange Resins (MeSH)</term><term>Chromatography, High Pressure Liquid (instrumentation)</term><term>Chromatography, High Pressure Liquid (methods)</term><term>Hydrogen-Ion Concentration (MeSH)</term><term>Isoelectric Focusing (MeSH)</term><term>Isoenzymes (isolation & purification)</term><term>Peroxidases (isolation & purification)</term><term>Phanerochaete (enzymology)</term><term>Salts (chemistry)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Salts</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Isoenzymes</term><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Anion Exchange Resins</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="instrumentation" xml:lang="en"><term>Chromatography, High Pressure Liquid</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Chromatography, High Pressure Liquid</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Hydrogen-Ion Concentration</term><term>Isoelectric Focusing</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Different chromatographic methods including chromatofocusing are used for separation of manganese peroxidase (MnP) isoforms and their isolation from the fungal growth medium. We tested strong anion exchange methacrylate based monolithic columns as a stationary phase for fast separation of MnP's. Sodium acetate buffers of two different pH values (6 and 4) were used for formation of reproducible pH gradient. The entire cycle, involving analysis and column regeneration, was completed in 3 min. Use of pH gradient showed better MnP isoform separation comparing to the salt gradient, while application of combined pH-salt gradient, resulted in further improvement.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">14670754</PMID><DateCompleted><Year>2004</Year><Month>04</Month><Day>15</Day></DateCompleted><DateRevised><Year>2019</Year><Month>09</Month><Day>22</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1570-0232</ISSN><JournalIssue CitedMedium="Print"><Volume>799</Volume><Issue>2</Issue><PubDate><Year>2004</Year><Month>Jan</Month><Day>25</Day></PubDate></JournalIssue><Title>Journal of chromatography. B, Analytical technologies in the biomedical and life sciences</Title><ISOAbbreviation>J Chromatogr B Analyt Technol Biomed Life Sci</ISOAbbreviation></Journal><ArticleTitle>Separation of manganese peroxidase isoenzymes on strong anion-exchange monolithic column using pH-salt gradient.</ArticleTitle><Pagination><MedlinePgn>343-7</MedlinePgn></Pagination><Abstract><AbstractText>Different chromatographic methods including chromatofocusing are used for separation of manganese peroxidase (MnP) isoforms and their isolation from the fungal growth medium. We tested strong anion exchange methacrylate based monolithic columns as a stationary phase for fast separation of MnP's. Sodium acetate buffers of two different pH values (6 and 4) were used for formation of reproducible pH gradient. The entire cycle, involving analysis and column regeneration, was completed in 3 min. Use of pH gradient showed better MnP isoform separation comparing to the salt gradient, while application of combined pH-salt gradient, resulted in further improvement.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Podgornik</LastName><ForeName>Helena</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>University of Ljubljana, Faculty of Chemistry and Chemical Technology, Askerceva 5, Ljubljana 1000, Slovenia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Podgornik</LastName><ForeName>Ales</ForeName><Initials>A</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>Netherlands</Country><MedlineTA>J Chromatogr B Analyt Technol Biomed Life Sci</MedlineTA><NlmUniqueID>101139554</NlmUniqueID><ISSNLinking>1570-0232</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000837">Anion Exchange Resins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007527">Isoenzymes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012492">Salts</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.13</RegistryNumber><NameOfSubstance UI="C051129">manganese peroxidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000837" MajorTopicYN="Y">Anion Exchange Resins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002851" MajorTopicYN="N">Chromatography, High Pressure Liquid</DescriptorName><QualifierName UI="Q000295" MajorTopicYN="Y">instrumentation</QualifierName><QualifierName UI="Q000379" MajorTopicYN="N">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007525" MajorTopicYN="N">Isoelectric Focusing</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007527" MajorTopicYN="N">Isoenzymes</DescriptorName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012492" MajorTopicYN="N">Salts</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2003</Year><Month>12</Month><Day>13</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2004</Year><Month>4</Month><Day>16</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2003</Year><Month>12</Month><Day>13</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">14670754</ArticleId><ArticleId IdType="pii">S1570023203009048</ArticleId><ArticleId IdType="doi">10.1016/j.jchromb.2003.10.059</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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