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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Purification, Characterization, and Immunological Properties for Two Isoforms of Glutathione Reductase from Eastern White Pine Needles <xref ref-type="fn" rid="fn1"><sup>1</sup></xref></title><author><name sortKey="Anderson, James V" sort="Anderson, James V" uniqKey="Anderson J" first="James V." last="Anderson">James V. Anderson</name></author><author><name sortKey="Hess, John L" sort="Hess, John L" uniqKey="Hess J" first="John L." last="Hess">John L. Hess</name></author><author><name sortKey="Chevone, Boris I" sort="Chevone, Boris I" uniqKey="Chevone B" first="Boris I." last="Chevone">Boris I. Chevone</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">16667845</idno><idno type="pmc">1077390</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1077390</idno><idno type="RBID">PMC:1077390</idno><date when="1990">1990</date><idno type="wicri:Area/Pmc/Corpus">000925</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Purification, Characterization, and Immunological Properties for Two Isoforms of Glutathione Reductase from Eastern White Pine Needles <xref ref-type="fn" rid="fn1"><sup>1</sup></xref></title><author><name sortKey="Anderson, James V" sort="Anderson, James V" uniqKey="Anderson J" first="James V." last="Anderson">James V. Anderson</name></author><author><name sortKey="Hess, John L" sort="Hess, John L" uniqKey="Hess J" first="John L." last="Hess">John L. Hess</name></author><author><name sortKey="Chevone, Boris I" sort="Chevone, Boris I" uniqKey="Chevone B" first="Boris I." last="Chevone">Boris I. Chevone</name></author></analytic><series><title level="j">Plant Physiology</title><idno type="ISSN">0032-0889</idno><idno type="eISSN">1532-2548</idno><imprint><date when="1990">1990</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Glutathione reductase (EC 1.6.4.2) was purified from Eastern white pine (<italic>Pinus strobus</italic> L.) needles. The purification steps included affinity chromatography using 2′, 5′-ADP-Sepharose, FPLC-anion-exchange, FPLC-hydrophobic interaction, and FPLC-gel filtration. Separation of proteins by FPLC-anion-exchange resulted in the recovery of two distinct isoforms of glutathione reductase (GR<sub>A</sub> and GR<sub>B</sub>). Purified GR<sub>A</sub> had a specific activity of 1.81 microkatals per milligram of protein and GR<sub>B</sub> had a specific activity of 6.08 microkatals per milligram of protein. GR<sub>A</sub> accounted for 17% of the total units of glutathione reductase recovered after anion-exchange separation and GR<sub>B</sub> accounted for 83%. The native molecular mass for GR<sub>A</sub> was 103 to 104 kilodaltons and for GR<sub>B</sub> was 88 to 95 kilodaltons. Both isoforms of glutathione reductase were dimers composed of identical subunit molecular masses which were 53 to 54 kilodaltons for GR<sub>A</sub> and 57 kilodaltons for GR<sub>B</sub>. The pH optimum for GR<sub>A</sub> was 7.25 to 7.75 and for GR<sub>B</sub> was 7.25. At 25°C the <italic>K</italic><sub>m</sub> for GSSG was 15.3 and 39.8 micromolar for GR<sub>A</sub> and GR<sub>B</sub>, respectively. For NADPH, the <italic>K</italic><sub>m</sub> was 3.7 and 8.8 micromolar for GR<sub>A</sub> and GR<sub>B</sub>, respectively. Antibody produced from purified GR<sub>B</sub> was reactive with both native and denatured GR<sub>B</sub>, but was cross-reactive with only native GR<sub>A</sub>.</p><sec sec-type="scanned-figures"><title>Images</title><fig id="F1"><label>Figure 3</label><graphic xlink:href="plntphys00812-0563-a" xlink:role="1405"></graphic></fig><fig id="F2"><label>Figure 4</label><graphic xlink:href="plntphys00812-0563-b" xlink:role="1405"></graphic></fig><fig id="F3"><label>Figure 5</label><graphic xlink:href="plntphys00812-0564-a" xlink:role="1406"></graphic></fig></sec></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Plant Physiol</journal-id><journal-title>Plant Physiology</journal-title><issn pub-type="ppub">0032-0889</issn><issn pub-type="epub">1532-2548</issn></journal-meta><article-meta><article-id pub-id-type="pmid">16667845</article-id><article-id pub-id-type="pmc">1077390</article-id><article-categories><subj-group subj-group-type="heading"><subject>Metabolism and Enzymology</subject></subj-group></article-categories><title-group><article-title>Purification, Characterization, and Immunological Properties for Two Isoforms of Glutathione Reductase from Eastern White Pine Needles <xref ref-type="fn" rid="fn1"><sup>1</sup></xref></article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Anderson</surname><given-names>James V.</given-names></name></contrib><contrib contrib-type="author"><name><surname>Hess</surname><given-names>John L.</given-names></name></contrib><contrib contrib-type="author"><name><surname>Chevone</surname><given-names>Boris I.</given-names></name></contrib></contrib-group><aff id="af1">Department of Plant Pathology, Physiology and Weed Science, Virginia Polytechnic Institute and State University Blacksburg, Virginia 24061</aff><aff id="af2">Department of Biochemistry and Nutrition, Virginia Polytechnic Institute and State University Blacksburg, Virginia 24061</aff><author-notes><fn id="fn1"><label>1</label><p> This research was supported by Environmental Protection Agency grant No. R-814224-01-0 to B. I. C. and J. L. H. This article has not been subjected to EPA peer and administrative review and may not necessarily reflect the views of EPA and no official endorsement should be inferred.</p></fn></author-notes><pub-date pub-type="ppub"><month>11</month><year>1990</year></pub-date><volume>94</volume><issue>3</issue><fpage>1402</fpage><lpage>1409</lpage><abstract><p>Glutathione reductase (EC 1.6.4.2) was purified from Eastern white pine (<italic>Pinus strobus</italic> L.) needles. The purification steps included affinity chromatography using 2′, 5′-ADP-Sepharose, FPLC-anion-exchange, FPLC-hydrophobic interaction, and FPLC-gel filtration. Separation of proteins by FPLC-anion-exchange resulted in the recovery of two distinct isoforms of glutathione reductase (GR<sub>A</sub> and GR<sub>B</sub>). Purified GR<sub>A</sub> had a specific activity of 1.81 microkatals per milligram of protein and GR<sub>B</sub> had a specific activity of 6.08 microkatals per milligram of protein. GR<sub>A</sub> accounted for 17% of the total units of glutathione reductase recovered after anion-exchange separation and GR<sub>B</sub> accounted for 83%. The native molecular mass for GR<sub>A</sub> was 103 to 104 kilodaltons and for GR<sub>B</sub> was 88 to 95 kilodaltons. Both isoforms of glutathione reductase were dimers composed of identical subunit molecular masses which were 53 to 54 kilodaltons for GR<sub>A</sub> and 57 kilodaltons for GR<sub>B</sub>. The pH optimum for GR<sub>A</sub> was 7.25 to 7.75 and for GR<sub>B</sub> was 7.25. At 25°C the <italic>K</italic><sub>m</sub> for GSSG was 15.3 and 39.8 micromolar for GR<sub>A</sub> and GR<sub>B</sub>, respectively. For NADPH, the <italic>K</italic><sub>m</sub> was 3.7 and 8.8 micromolar for GR<sub>A</sub> and GR<sub>B</sub>, respectively. Antibody produced from purified GR<sub>B</sub> was reactive with both native and denatured GR<sub>B</sub>, but was cross-reactive with only native GR<sub>A</sub>.</p><sec sec-type="scanned-figures"><title>Images</title><fig id="F1"><label>Figure 3</label><graphic xlink:href="plntphys00812-0563-a" xlink:role="1405"></graphic></fig><fig id="F2"><label>Figure 4</label><graphic xlink:href="plntphys00812-0563-b" xlink:role="1405"></graphic></fig><fig id="F3"><label>Figure 5</label><graphic xlink:href="plntphys00812-0564-a" xlink:role="1406"></graphic></fig></sec></abstract></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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