Metabolism of uronic acids in plant tissues: partial purification and properties of uronic Acid oxidase from citrus leaves.
Identifieur interne : 001006 ( PubMed/Curation ); précédent : 001005; suivant : 001007Metabolism of uronic acids in plant tissues: partial purification and properties of uronic Acid oxidase from citrus leaves.
Auteurs : J. Riov [Israël]Source :
- Plant physiology [ 0032-0889 ] ; 1975.
Abstract
A new enzyme, named uronic acid oxidase, was extracted and purified 67-fold by (NH(4))(2)SO(4) fractionation and CM-Sephadex column chromatography from ethylene-treated Shamouti orange (Citrus sinensis L. Osbeck) leaves. The enzyme catalyzes the oxidation of d-galacturonic acid and d-glucuronic acid to the corresponding hexaric acids in the presence of molecular oxygen with the production of H(2)O(2). The pH optimum for the oxidation of d-galacturonic acid and d-glucuronic acid is between 7 and 8. The enzyme is highly specific for d-galacturonic acid and d-glucuronic acid. It also oxidizes polygalacturonic acid. The apparent Michaelis constant values of the enzyme for d-galacturonic acid and d-glucuronic acid are 0.13 and 0.5 mm, respectively. The molecular weight of the enzyme, as determined by gel filtration, is about 98,000. The enzyme is inhibited by sodium hydrosulfite and other sulfites, indicating that it contains a flavin prosthetic group.
PubMed: 16659133
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Riov</name><affiliation wicri:level="1"><nlm:affiliation>Department of Horticulture, The Hebrew University of Jerusalem, Rehovot, Israel.</nlm:affiliation><country xml:lang="fr">Israël</country><wicri:regionArea>Department of Horticulture, The Hebrew University of Jerusalem, Rehovot</wicri:regionArea></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1975">1975</date><idno type="RBID">pubmed:16659133</idno><idno type="pmid">16659133</idno><idno type="wicri:Area/PubMed/Corpus">001006</idno><idno type="wicri:Area/PubMed/Curation">001006</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Metabolism of uronic acids in plant tissues: partial purification and properties of uronic Acid oxidase from citrus leaves.</title><author><name sortKey="Riov, J" sort="Riov, J" uniqKey="Riov J" first="J" last="Riov">J. Riov</name><affiliation wicri:level="1"><nlm:affiliation>Department of Horticulture, The Hebrew University of Jerusalem, Rehovot, Israel.</nlm:affiliation><country xml:lang="fr">Israël</country><wicri:regionArea>Department of Horticulture, The Hebrew University of Jerusalem, Rehovot</wicri:regionArea></affiliation></author></analytic><series><title level="j">Plant physiology</title><idno type="ISSN">0032-0889</idno><imprint><date when="1975" type="published">1975</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A new enzyme, named uronic acid oxidase, was extracted and purified 67-fold by (NH(4))(2)SO(4) fractionation and CM-Sephadex column chromatography from ethylene-treated Shamouti orange (Citrus sinensis L. Osbeck) leaves. The enzyme catalyzes the oxidation of d-galacturonic acid and d-glucuronic acid to the corresponding hexaric acids in the presence of molecular oxygen with the production of H(2)O(2). The pH optimum for the oxidation of d-galacturonic acid and d-glucuronic acid is between 7 and 8. The enzyme is highly specific for d-galacturonic acid and d-glucuronic acid. It also oxidizes polygalacturonic acid. The apparent Michaelis constant values of the enzyme for d-galacturonic acid and d-glucuronic acid are 0.13 and 0.5 mm, respectively. The molecular weight of the enzyme, as determined by gel filtration, is about 98,000. The enzyme is inhibited by sodium hydrosulfite and other sulfites, indicating that it contains a flavin prosthetic group.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">16659133</PMID><DateCreated><Year>2010</Year><Month>6</Month><Day>29</Day></DateCreated><DateCompleted><Year>2010</Year><Month>06</Month><Day>29</Day></DateCompleted><DateRevised><Year>2010</Year><Month>9</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0032-0889</ISSN><JournalIssue CitedMedium="Print"><Volume>55</Volume><Issue>4</Issue><PubDate><Year>1975</Year><Month>Apr</Month></PubDate></JournalIssue><Title>Plant physiology</Title><ISOAbbreviation>Plant Physiol.</ISOAbbreviation></Journal><ArticleTitle>Metabolism of uronic acids in plant tissues: partial purification and properties of uronic Acid oxidase from citrus leaves.</ArticleTitle><Pagination><MedlinePgn>602-6</MedlinePgn></Pagination><Abstract><AbstractText>A new enzyme, named uronic acid oxidase, was extracted and purified 67-fold by (NH(4))(2)SO(4) fractionation and CM-Sephadex column chromatography from ethylene-treated Shamouti orange (Citrus sinensis L. Osbeck) leaves. The enzyme catalyzes the oxidation of d-galacturonic acid and d-glucuronic acid to the corresponding hexaric acids in the presence of molecular oxygen with the production of H(2)O(2). The pH optimum for the oxidation of d-galacturonic acid and d-glucuronic acid is between 7 and 8. The enzyme is highly specific for d-galacturonic acid and d-glucuronic acid. It also oxidizes polygalacturonic acid. The apparent Michaelis constant values of the enzyme for d-galacturonic acid and d-glucuronic acid are 0.13 and 0.5 mm, respectively. The molecular weight of the enzyme, as determined by gel filtration, is about 98,000. The enzyme is inhibited by sodium hydrosulfite and other sulfites, indicating that it contains a flavin prosthetic group.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Riov</LastName><ForeName>J</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Department of Horticulture, The Hebrew University of Jerusalem, Rehovot, Israel.</Affiliation></AffiliationInfo></Author></AuthorList><Language>ENG</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Plant Physiol</MedlineTA><NlmUniqueID>0401224</NlmUniqueID><ISSNLinking>0032-0889</ISSNLinking></MedlineJournalInfo><CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 1951 Nov;193(1):265-75</RefSource><PMID Version="1">14907713</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Bacteriol. 1969 Sep;99(3):667-73</RefSource><PMID Version="1">4313130</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Bacteriol. 1970 Apr;102(1):85-96</RefSource><PMID Version="1">4314480</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 1969 Aug 10;244(15):3999-4006</RefSource><PMID Version="1">4389773</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Arch Biochem Biophys. 1970 Jan;136(1):97-105</RefSource><PMID Version="1">4392089</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Biochem. 1966 Mar;59(3):216-22</RefSource><PMID Version="1">5944335</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 1961 Feb;236:308-12</RefSource><PMID Version="1">13752745</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Biochem Biophys Res Commun. 1963 May 3;11:239-43</RefSource><PMID Version="1">13971911</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Fed Proc. 1964 Jan-Feb;23:18-29</RefSource><PMID Version="1">14114688</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Arch Biochem Biophys. 1961 Dec;95:483-93</RefSource><PMID Version="1">14466265</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Nature. 1950 Sep 9;166(4219):444-5</RefSource><PMID Version="1">14775715</PMID></CommentsCorrections></CommentsCorrectionsList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1975</Year><Month>4</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1975</Year><Month>4</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1975</Year><Month>4</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">16659133</ArticleId><ArticleId IdType="pmc">PMC541672</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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