Effects of salicylate and other benzoates on oxidative enzymes of the tricarboxylic acid cycle in rat tissue homogenates
Identifieur interne : 003874 ( Istex/Corpus ); précédent : 003873; suivant : 003875Effects of salicylate and other benzoates on oxidative enzymes of the tricarboxylic acid cycle in rat tissue homogenates
Auteurs : E. H. Kaplan ; Jean Kennedy ; Jane DavisSource :
- Archives of Biochemistry and Biophysics [ 0003-9861 ] ; 1953.
Abstract
Salicylate and related compounds inhibit the Krebs cycle in kidney and liver homogenates. The oxidative enzymes inhibited to the greatest extent are α-ketoglutaric dehydrogenase and succinic dehydrogenase. Inhibition of the former is reversed by the presence of an excess of magnesium ions. The two enzymes also differ in the relative inhibitory effects of other substances chemically related to salicylate. Inhibition of oxidation of succinate is also reversible, but the factor which reverses this inhibition is unknown. When magnesium is present in excess, salicylate may enhance oxidative activity.
Url:
DOI: 10.1016/0003-9861(54)90452-X
Links to Exploration step
ISTEX:050D61C180A73CD284E3898C17259829D24D877FLe document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Effects of salicylate and other benzoates on oxidative enzymes of the tricarboxylic acid cycle in rat tissue homogenates</title><author><name sortKey="Kaplan, E H" sort="Kaplan, E H" uniqKey="Kaplan E" first="E. H." last="Kaplan">E. H. Kaplan</name><affiliation><mods:affiliation>From the Rheumatic Fever Research Institute, Northwestern University Medical School, Chicago, Illinois, USA</mods:affiliation></affiliation></author><author><name sortKey="Kennedy, Jean" sort="Kennedy, Jean" uniqKey="Kennedy J" first="Jean" last="Kennedy">Jean Kennedy</name><affiliation><mods:affiliation>From the Rheumatic Fever Research Institute, Northwestern University Medical School, Chicago, Illinois, USA</mods:affiliation></affiliation></author><author><name sortKey="Davis, Jane" sort="Davis, Jane" uniqKey="Davis J" first="Jane" last="Davis">Jane Davis</name><affiliation><mods:affiliation>From the Rheumatic Fever Research Institute, Northwestern University Medical School, Chicago, Illinois, USA</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:050D61C180A73CD284E3898C17259829D24D877F</idno><date when="1954" year="1954">1954</date><idno type="doi">10.1016/0003-9861(54)90452-X</idno><idno type="url">https://api.istex.fr/document/050D61C180A73CD284E3898C17259829D24D877F/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">003874</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Effects of salicylate and other benzoates on oxidative enzymes of the tricarboxylic acid cycle in rat tissue homogenates</title><author><name sortKey="Kaplan, E H" sort="Kaplan, E H" uniqKey="Kaplan E" first="E. H." last="Kaplan">E. H. Kaplan</name><affiliation><mods:affiliation>From the Rheumatic Fever Research Institute, Northwestern University Medical School, Chicago, Illinois, USA</mods:affiliation></affiliation></author><author><name sortKey="Kennedy, Jean" sort="Kennedy, Jean" uniqKey="Kennedy J" first="Jean" last="Kennedy">Jean Kennedy</name><affiliation><mods:affiliation>From the Rheumatic Fever Research Institute, Northwestern University Medical School, Chicago, Illinois, USA</mods:affiliation></affiliation></author><author><name sortKey="Davis, Jane" sort="Davis, Jane" uniqKey="Davis J" first="Jane" last="Davis">Jane Davis</name><affiliation><mods:affiliation>From the Rheumatic Fever Research Institute, Northwestern University Medical School, Chicago, Illinois, USA</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Archives of Biochemistry and Biophysics</title><title level="j" type="abbrev">YABBI</title><idno type="ISSN">0003-9861</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1953">1953</date><biblScope unit="volume">51</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="47">47</biblScope><biblScope unit="page" to="61">61</biblScope></imprint><idno type="ISSN">0003-9861</idno></series><idno type="istex">050D61C180A73CD284E3898C17259829D24D877F</idno><idno type="DOI">10.1016/0003-9861(54)90452-X</idno><idno type="PII">0003-9861(54)90452-X</idno><idno type="ArticleID">5490452X</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0003-9861</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Salicylate and related compounds inhibit the Krebs cycle in kidney and liver homogenates. The oxidative enzymes inhibited to the greatest extent are α-ketoglutaric dehydrogenase and succinic dehydrogenase. Inhibition of the former is reversed by the presence of an excess of magnesium ions. The two enzymes also differ in the relative inhibitory effects of other substances chemically related to salicylate. Inhibition of oxidation of succinate is also reversible, but the factor which reverses this inhibition is unknown. When magnesium is present in excess, salicylate may enhance oxidative activity.</div></front></TEI><istex><corpusName>elsevier</corpusName><author><json:item><name>E.H. Kaplan</name><affiliations><json:string>From the Rheumatic Fever Research Institute, Northwestern University Medical School, Chicago, Illinois, USA</json:string></affiliations></json:item><json:item><name>Jean Kennedy</name><affiliations><json:string>From the Rheumatic Fever Research Institute, Northwestern University Medical School, Chicago, Illinois, USA</json:string></affiliations></json:item><json:item><name>Jane Davis</name><affiliations><json:string>From the Rheumatic Fever Research Institute, Northwestern University Medical School, Chicago, Illinois, USA</json:string></affiliations></json:item></author><articleId><json:string>5490452X</json:string></articleId><language><json:string>eng</json:string></language><abstract>Salicylate and related compounds inhibit the Krebs cycle in kidney and liver homogenates. The oxidative enzymes inhibited to the greatest extent are α-ketoglutaric dehydrogenase and succinic dehydrogenase. Inhibition of the former is reversed by the presence of an excess of magnesium ions. The two enzymes also differ in the relative inhibitory effects of other substances chemically related to salicylate. Inhibition of oxidation of succinate is also reversible, but the factor which reverses this inhibition is unknown. When magnesium is present in excess, salicylate may enhance oxidative activity.</abstract><qualityIndicators><score>5.03</score><pdfVersion>1.3</pdfVersion><pdfPageSize>396 x 576 pts</pdfPageSize><refBibsNative>true</refBibsNative><keywordCount>0</keywordCount><abstractCharCount>602</abstractCharCount><pdfWordCount>3986</pdfWordCount><pdfCharCount>24660</pdfCharCount><pdfPageCount>15</pdfPageCount><abstractWordCount>87</abstractWordCount></qualityIndicators><title>Effects of salicylate and other benzoates on oxidative enzymes of the tricarboxylic acid cycle in rat tissue homogenates</title><pii><json:string>0003-9861(54)90452-X</json:string></pii><genre><json:string>research-article</json:string></genre><host><volume>51</volume><pii><json:string>S0003-9861(00)X0671-6</json:string></pii><pages><last>61</last><first>47</first></pages><issn><json:string>0003-9861</json:string></issn><issue>1</issue><genre><json:string>Journal</json:string></genre><language><json:string>unknown</json:string></language><title>Archives of Biochemistry and Biophysics</title><publicationDate>1954</publicationDate></host><publicationDate>1953</publicationDate><copyrightDate>1954</copyrightDate><doi><json:string>10.1016/0003-9861(54)90452-X</json:string></doi><id>050D61C180A73CD284E3898C17259829D24D877F</id><fulltext><json:item><original>true</original><mimetype>application/pdf</mimetype><extension>pdf</extension><uri>https://api.istex.fr/document/050D61C180A73CD284E3898C17259829D24D877F/fulltext/pdf</uri></json:item><json:item><original>true</original><mimetype>text/plain</mimetype><extension>txt</extension><uri>https://api.istex.fr/document/050D61C180A73CD284E3898C17259829D24D877F/fulltext/txt</uri></json:item><json:item><original>false</original><mimetype>application/zip</mimetype><extension>zip</extension><uri>https://api.istex.fr/document/050D61C180A73CD284E3898C17259829D24D877F/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/050D61C180A73CD284E3898C17259829D24D877F/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">Effects of salicylate and other benzoates on oxidative enzymes of the tricarboxylic acid cycle in rat tissue homogenates</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>ELSEVIER</publisher><availability><p>ELSEVIER</p></availability><date>1954</date></publicationStmt><notesStmt><note>This work was supported in part by a grant from the U. S. Public Health Service.</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">Effects of salicylate and other benzoates on oxidative enzymes of the tricarboxylic acid cycle in rat tissue homogenates</title><author><persName><forename type="first">E.H.</forename><surname>Kaplan</surname></persName><affiliation>From the Rheumatic Fever Research Institute, Northwestern University Medical School, Chicago, Illinois, USA</affiliation></author><author><persName><forename type="first">Jean</forename><surname>Kennedy</surname></persName><affiliation>From the Rheumatic Fever Research Institute, Northwestern University Medical School, Chicago, Illinois, USA</affiliation></author><author><persName><forename type="first">Jane</forename><surname>Davis</surname></persName><affiliation>From the Rheumatic Fever Research Institute, Northwestern University Medical School, Chicago, Illinois, USA</affiliation></author></analytic><monogr><title level="j">Archives of Biochemistry and Biophysics</title><title level="j" type="abbrev">YABBI</title><idno type="pISSN">0003-9861</idno><idno type="PII">S0003-9861(00)X0671-6</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1953"></date><biblScope unit="volume">51</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="47">47</biblScope><biblScope unit="page" to="61">61</biblScope></imprint></monogr><idno type="istex">050D61C180A73CD284E3898C17259829D24D877F</idno><idno type="DOI">10.1016/0003-9861(54)90452-X</idno><idno type="PII">0003-9861(54)90452-X</idno><idno type="ArticleID">5490452X</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1954</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Salicylate and related compounds inhibit the Krebs cycle in kidney and liver homogenates. The oxidative enzymes inhibited to the greatest extent are α-ketoglutaric dehydrogenase and succinic dehydrogenase. Inhibition of the former is reversed by the presence of an excess of magnesium ions. The two enzymes also differ in the relative inhibitory effects of other substances chemically related to salicylate. Inhibition of oxidation of succinate is also reversible, but the factor which reverses this inhibition is unknown. When magnesium is present in excess, salicylate may enhance oxidative activity.</p></abstract></profileDesc><revisionDesc><change when="1953-08-20">Received</change><change when="1953">Published</change></revisionDesc></teiHeader></istex:fulltextTEI></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="UTF-8"</istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType><istex:document><converted-article version="4.5.2" docsubtype="fla" xml:lang="en"><item-info><jid>YABBI</jid><aid>5490452X</aid><ce:pii>0003-9861(54)90452-X</ce:pii><ce:doi>10.1016/0003-9861(54)90452-X</ce:doi><ce:copyright type="unknown" year="1954"></ce:copyright></item-info><head><ce:article-footnote><ce:label>☆</ce:label><ce:note-para>This work was supported in part by a grant from the U. S. Public Health Service.</ce:note-para></ce:article-footnote><ce:title>Effects of salicylate and other benzoates on oxidative enzymes of the tricarboxylic acid cycle in rat tissue homogenates</ce:title><ce:author-group><ce:author><ce:given-name>E.H.</ce:given-name><ce:surname>Kaplan</ce:surname></ce:author><ce:author><ce:given-name>Jean</ce:given-name><ce:surname>Kennedy</ce:surname></ce:author><ce:author><ce:given-name>Jane</ce:given-name><ce:surname>Davis</ce:surname></ce:author><ce:affiliation><ce:textfn>From the Rheumatic Fever Research Institute, Northwestern University Medical School, Chicago, Illinois, USA</ce:textfn></ce:affiliation></ce:author-group><ce:date-received day="20" month="8" year="1953"></ce:date-received><ce:abstract class="author"><ce:section-title>Abstract</ce:section-title><ce:abstract-sec><ce:simple-para view="all" id="simple-para.0010">Salicylate and related compounds inhibit the Krebs cycle in kidney and liver homogenates. The oxidative enzymes inhibited to the greatest extent are α-ketoglutaric dehydrogenase and succinic dehydrogenase. Inhibition of the former is reversed by the presence of an excess of magnesium ions. The two enzymes also differ in the relative inhibitory effects of other substances chemically related to salicylate. Inhibition of oxidation of succinate is also reversible, but the factor which reverses this inhibition is unknown. When magnesium is present in excess, salicylate may enhance oxidative activity.</ce:simple-para></ce:abstract-sec></ce:abstract></head></converted-article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Effects of salicylate and other benzoates on oxidative enzymes of the tricarboxylic acid cycle in rat tissue homogenates</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>Effects of salicylate and other benzoates on oxidative enzymes of the tricarboxylic acid cycle in rat tissue homogenates</title></titleInfo><name type="personal"><namePart type="given">E.H.</namePart><namePart type="family">Kaplan</namePart><affiliation>From the Rheumatic Fever Research Institute, Northwestern University Medical School, Chicago, Illinois, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Jean</namePart><namePart type="family">Kennedy</namePart><affiliation>From the Rheumatic Fever Research Institute, Northwestern University Medical School, Chicago, Illinois, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Jane</namePart><namePart type="family">Davis</namePart><affiliation>From the Rheumatic Fever Research Institute, Northwestern University Medical School, Chicago, Illinois, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article"></genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1953</dateIssued><dateCaptured encoding="w3cdtf">1953-08-20</dateCaptured><copyrightDate encoding="w3cdtf">1954</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType></physicalDescription><abstract lang="en">Salicylate and related compounds inhibit the Krebs cycle in kidney and liver homogenates. The oxidative enzymes inhibited to the greatest extent are α-ketoglutaric dehydrogenase and succinic dehydrogenase. Inhibition of the former is reversed by the presence of an excess of magnesium ions. The two enzymes also differ in the relative inhibitory effects of other substances chemically related to salicylate. Inhibition of oxidation of succinate is also reversible, but the factor which reverses this inhibition is unknown. When magnesium is present in excess, salicylate may enhance oxidative activity.</abstract><note>This work was supported in part by a grant from the U. S. Public Health Service.</note><relatedItem type="host"><titleInfo><title>Archives of Biochemistry and Biophysics</title></titleInfo><titleInfo type="abbreviated"><title>YABBI</title></titleInfo><genre type="Journal">journal</genre><originInfo><dateIssued encoding="w3cdtf">195407</dateIssued></originInfo><identifier type="ISSN">0003-9861</identifier><identifier type="PII">S0003-9861(00)X0671-6</identifier><part><date>195407</date><detail type="volume"><number>51</number><caption>vol.</caption></detail><detail type="issue"><number>1</number><caption>no.</caption></detail><extent unit="issue pages"><start>1</start><end>318</end></extent><extent unit="pages"><start>47</start><end>61</end></extent></part></relatedItem><identifier type="istex">050D61C180A73CD284E3898C17259829D24D877F</identifier><identifier type="DOI">10.1016/0003-9861(54)90452-X</identifier><identifier type="PII">0003-9861(54)90452-X</identifier><identifier type="ArticleID">5490452X</identifier><recordInfo><recordContentSource>ELSEVIER</recordContentSource></recordInfo></mods></metadata><enrichments><istex:refBibTEI uri="https://api.istex.fr/document/050D61C180A73CD284E3898C17259829D24D877F/enrichments/refBib"><teiHeader></teiHeader><text><front></front><body></body><back><listBibl><biblStruct><analytic><author><persName><forename type="first">S</forename><surname>Mahlen</surname></persName></author></analytic><monogr><title level="j">Skand. Arch. Physiol</title><imprint><biblScope unit="volume">63</biblScope><biblScope unit="issue">152</biblScope><date type="published" when="1928"></date></imprint></monogr></biblStruct><biblStruct><analytic><author><persName><forename type="first">M</forename><forename type="middle">E</forename><surname>Collett</surname></persName></author><author><persName><forename type="middle">F</forename><surname>And Clarke</surname></persName></author></analytic><monogr><title level="j">J. Biol. Chem</title><imprint><biblScope unit="volume">82</biblScope><biblScope unit="page">429</biblScope><date type="published" when="1929"></date></imprint></monogr></biblStruct><biblStruct><analytic><author><persName><forename type="first">W</forename><forename type="middle">H</forename><surname>Griffith</surname></persName></author><author><persName><surname>Sot</surname></persName></author></analytic><monogr><title level="j">Biol. Med</title><imprint><biblScope unit="volume">37</biblScope><biblScope unit="page">279</biblScope><date type="published" when="1937"></date></imprint></monogr></biblStruct><biblStruct><analytic><author><persName><forename type="first">J</forename><forename type="middle">R</forename><surname>Klein</surname></persName></author><author><persName><forename type="first">H</forename><surname>And Kamin</surname></persName></author></analytic><monogr><title level="j">J. Biol. Chem</title><imprint><biblScope unit="volume">138</biblScope><biblScope unit="page">507</biblScope><date type="published" when="1941"></date></imprint></monogr></biblStruct><biblStruct><analytic><author><persName><forename type="first">B</forename><surname>Herner</surname></persName></author></analytic><monogr><title level="j">Acta Physiol. &and</title><imprint><biblScope unit="volume">4</biblScope><biblScope unit="page">76</biblScope><date type="published" when="1942"></date></imprint></monogr></biblStruct><biblStruct><analytic><author><persName><forename type="first">B</forename><surname>Herner</surname></persName></author></analytic><monogr><title level="j">Acta Physiol. Scan&</title><imprint><biblScope unit="volume">8</biblScope><biblScope unit="issue">23</biblScope><date type="published" when="1944"></date></imprint></monogr><note>Suppl</note></biblStruct><biblStruct><analytic><author><persName><forename type="first">Von</forename><surname>Euler</surname></persName></author><author><persName><forename type="first">H</forename></persName></author></analytic><monogr><title level="j">Ber. deut. Chem. Ges</title><imprint><biblScope unit="volume">76</biblScope><biblScope unit="page">1876</biblScope><date type="published" when="1942"></date></imprint></monogr></biblStruct><biblStruct><analytic><author><persName><forename type="first">E</forename><surname>Adler</surname></persName></author><author><persName><forename type="first">H</forename><surname>Von Euler</surname></persName></author><author><persName><forename type="first">B</forename><surname>And Skarzynski</surname></persName></author></analytic><monogr><title level="j">Arkiv Kemi, Mineral. Geol</title><imprint><biblScope unit="volume">16</biblScope><biblScope unit="issue">9</biblScope><date type="published" when="1942"></date></imprint></monogr></biblStruct><biblStruct><analytic><author><persName><forename type="first">Von</forename><surname>Euler</surname></persName></author><author><persName><forename type="first">H</forename><surname>And Allstr~m</surname></persName></author><author><persName><forename type="first">L</forename></persName></author></analytic><monogr><title level="j">Arkiv Kemi, Mineral. Geol</title><imprint><biblScope unit="volume">16</biblScope><biblScope unit="issue">16</biblScope><date type="published" when="1943"></date></imprint></monogr></biblStruct><biblStruct><analytic><author><persName><forename type="first">Von</forename><surname>Euler</surname></persName></author><author><persName><forename type="first">H</forename><surname>And Allstr~m</surname></persName></author><author><persName><forename type="first">L</forename></persName></author></analytic><monogr><title level="j">physiol. Chem</title><imprint><biblScope unit="volume">2</biblScope><biblScope unit="issue">279</biblScope><biblScope unit="page">175</biblScope><date type="published" when="1943"></date></imprint></monogr></biblStruct><biblStruct><analytic><author><persName><forename type="first">N</forename><surname>Alwall</surname></persName></author></analytic><monogr><title level="j">Skand. Arch. Physiol</title><imprint><biblScope unit="volume">80</biblScope><biblScope unit="issue">27</biblScope><date type="published" when="1938"></date></imprint></monogr></biblStruct><biblStruct><analytic></analytic><monogr><title level="j">TRICARBOXYLIC ACID CYCLE STUDIES</title></monogr></biblStruct></listBibl></back></text></istex:refBibTEI></enrichments><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Informatique/explor/ScrumV1/Data/Istex/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 003874 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Istex/Corpus/biblio.hfd -nk 003874 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Wicri/Informatique
|area= ScrumV1
|flux= Istex
|étape= Corpus
|type= RBID
|clé= ISTEX:050D61C180A73CD284E3898C17259829D24D877F
|texte= Effects of salicylate and other benzoates on oxidative enzymes of the tricarboxylic acid cycle in rat tissue homogenates
}}
| This area was generated with Dilib version V0.6.39. |  |