Close resemblance between muscle pyruvate kinase from a primitive vertebrate, the river sturgeon Acipenser fulvenscens , and the ancestral type K isozyme
Identifieur interne : 001198 ( Istex/Corpus ); précédent : 001197; suivant : 001199Close resemblance between muscle pyruvate kinase from a primitive vertebrate, the river sturgeon Acipenser fulvenscens , and the ancestral type K isozyme
Auteurs : Helga Guderley ; Lucie Hamel ; Julie LafondSource :
- Journal of comparative physiology [ 0340-7594 ] ; 1983-06-01.
Abstract
Summary: Pyruvate kinase (PK) exists as at least two electrophoretically distinguishable, tissue specific form in the river sturgeonAcipenser fulvenscens. In contrast with the PK isozyme system in other vertebrates, the isozyme present in muscle is also present in non-musclce tissues, notably the spleen. The presence of a five membered set of hybrids in liver, gills, eyes and intestine suggests that the synthesis of this isozyme occurs in other tissues as well. Thus, in this primitive vertebrate, the specialization of one PK isozyme for function in muscle tissues is not complete. Sturgeon muscle PK had slightly cooperative phosphoenolpyruvate (PEP) saturation curves (S0.5=0.33 mM) and a Hill coefficient,n H, of 1.24, and was strongly activated by fructose 1,6 bisphosphate (PEP S0.5=0.098 mM;n H=1.0). The enzyme was strongly inhibited by phenylalanine, alanine and MgATP. Fructose 1,6 bisphosphate (FBP) not only totally reversed these inhibitory effects, but also activated the enzyme to the same extent as in the absence of the inhibitors. These kinetic properties closely resemble those of vertebrate type K pyruvate kinases, and are quite distinct from those of higher vertebrate type M isozymes. Nevertheless, immunotitration studies indicate structural homology among the sturgeon, frog and dog muscle PK's as they are all precipitated by antisera to the other forms. This maintenance of structural homology, despite a marked degree of functional differentiation, suggests that only small structural modifications were required to generate the functionally specialized forms of muscle PK found among the vertebrates.
Url:
DOI: 10.1007/BF00689628
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ISTEX:94802A6C84D2E1218F9C28F21BDD71DE848FA423Le document en format XML
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In contrast with the PK isozyme system in other vertebrates, the isozyme present in muscle is also present in non-musclce tissues, notably the spleen. The presence of a five membered set of hybrids in liver, gills, eyes and intestine suggests that the synthesis of this isozyme occurs in other tissues as well. Thus, in this primitive vertebrate, the specialization of one PK isozyme for function in muscle tissues is not complete. Sturgeon muscle PK had slightly cooperative phosphoenolpyruvate (PEP) saturation curves (S0.5=0.33 mM) and a Hill coefficient,n H, of 1.24, and was strongly activated by fructose 1,6 bisphosphate (PEP S0.5=0.098 mM;n H=1.0). The enzyme was strongly inhibited by phenylalanine, alanine and MgATP. Fructose 1,6 bisphosphate (FBP) not only totally reversed these inhibitory effects, but also activated the enzyme to the same extent as in the absence of the inhibitors. These kinetic properties closely resemble those of vertebrate type K pyruvate kinases, and are quite distinct from those of higher vertebrate type M isozymes. Nevertheless, immunotitration studies indicate structural homology among the sturgeon, frog and dog muscle PK's as they are all precipitated by antisera to the other forms. This maintenance of structural homology, despite a marked degree of functional differentiation, suggests that only small structural modifications were required to generate the functionally specialized forms of muscle PK found among the vertebrates.</div></front></TEI><istex><corpusName>springer</corpusName><author><json:item><name>Helga Guderley</name><affiliations><json:string>Department de Biologie, Université Laval, GIK 7P4, Québec, Canada</json:string></affiliations></json:item><json:item><name>Lucie Hamel</name><affiliations><json:string>Department de Biologie, Université Laval, GIK 7P4, Québec, Canada</json:string></affiliations></json:item><json:item><name>Julie Lafond</name><affiliations><json:string>Department de Biologie, Université Laval, GIK 7P4, Québec, Canada</json:string></affiliations></json:item></author><articleId><json:string>BF00689628</json:string><json:string>Art12</json:string></articleId><language><json:string>eng</json:string></language><originalGenre><json:string>OriginalPaper</json:string></originalGenre><abstract>Summary: Pyruvate kinase (PK) exists as at least two electrophoretically distinguishable, tissue specific form in the river sturgeonAcipenser fulvenscens. In contrast with the PK isozyme system in other vertebrates, the isozyme present in muscle is also present in non-musclce tissues, notably the spleen. The presence of a five membered set of hybrids in liver, gills, eyes and intestine suggests that the synthesis of this isozyme occurs in other tissues as well. Thus, in this primitive vertebrate, the specialization of one PK isozyme for function in muscle tissues is not complete. Sturgeon muscle PK had slightly cooperative phosphoenolpyruvate (PEP) saturation curves (S0.5=0.33 mM) and a Hill coefficient,n H, of 1.24, and was strongly activated by fructose 1,6 bisphosphate (PEP S0.5=0.098 mM;n H=1.0). The enzyme was strongly inhibited by phenylalanine, alanine and MgATP. Fructose 1,6 bisphosphate (FBP) not only totally reversed these inhibitory effects, but also activated the enzyme to the same extent as in the absence of the inhibitors. These kinetic properties closely resemble those of vertebrate type K pyruvate kinases, and are quite distinct from those of higher vertebrate type M isozymes. Nevertheless, immunotitration studies indicate structural homology among the sturgeon, frog and dog muscle PK's as they are all precipitated by antisera to the other forms. This maintenance of structural homology, despite a marked degree of functional differentiation, suggests that only small structural modifications were required to generate the functionally specialized forms of muscle PK found among the vertebrates.</abstract><qualityIndicators><score>7.88</score><pdfVersion>1.3</pdfVersion><pdfPageSize>597.28 x 785 pts</pdfPageSize><refBibsNative>false</refBibsNative><keywordCount>0</keywordCount><abstractCharCount>1633</abstractCharCount><pdfWordCount>6715</pdfWordCount><pdfCharCount>37543</pdfCharCount><pdfPageCount>10</pdfPageCount><abstractWordCount>240</abstractWordCount></qualityIndicators><title>Close resemblance between muscle pyruvate kinase from a primitive vertebrate, the river sturgeon Acipenser fulvenscens , and the ancestral type K 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ancestral type K isozyme</title><respStmt><resp>Références bibliographiques récupérées via GROBID</resp><name resp="ISTEX-API">ISTEX-API (INIST-CNRS)</name></respStmt><respStmt><resp>Références bibliographiques récupérées via GROBID</resp><name resp="ISTEX-API">ISTEX-API (INIST-CNRS)</name></respStmt></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>Springer-Verlag</publisher><pubPlace>Berlin/Heidelberg</pubPlace><availability><p>Springer-Verlag, 1983</p></availability><date>1983</date></publicationStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">Close resemblance between muscle pyruvate kinase from a primitive vertebrate, the river sturgeon Acipenser fulvenscens , and the ancestral type K isozyme</title><author xml:id="author-1"><persName><forename type="first">Helga</forename><surname>Guderley</surname></persName><affiliation>Department de Biologie, Université Laval, GIK 7P4, Québec, Canada</affiliation></author><author xml:id="author-2"><persName><forename type="first">Lucie</forename><surname>Hamel</surname></persName><affiliation>Department de Biologie, Université Laval, GIK 7P4, Québec, Canada</affiliation></author><author xml:id="author-3"><persName><forename type="first">Julie</forename><surname>Lafond</surname></persName><affiliation>Department de Biologie, Université Laval, GIK 7P4, Québec, Canada</affiliation></author></analytic><monogr><title level="j">Journal of comparative physiology</title><title level="j" type="abbrev">J Comp Physiol B</title><idno type="journal-ID">359</idno><idno type="pISSN">0340-7594</idno><idno type="eISSN">1432-1351</idno><idno type="issue-article-count">15</idno><idno type="volume-issue-count">4</idno><imprint><publisher>Springer-Verlag</publisher><pubPlace>Berlin/Heidelberg</pubPlace><date type="published" when="1983-06-01"></date><biblScope unit="volume">153</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" 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In contrast with the PK isozyme system in other vertebrates, the isozyme present in muscle is also present in non-musclce tissues, notably the spleen. The presence of a five membered set of hybrids in liver, gills, eyes and intestine suggests that the synthesis of this isozyme occurs in other tissues as well. Thus, in this primitive vertebrate, the specialization of one PK isozyme for function in muscle tissues is not complete. Sturgeon muscle PK had slightly cooperative phosphoenolpyruvate (PEP) saturation curves (S0.5=0.33 mM) and a Hill coefficient,n H, of 1.24, and was strongly activated by fructose 1,6 bisphosphate (PEP S0.5=0.098 mM;n H=1.0). The enzyme was strongly inhibited by phenylalanine, alanine and MgATP. Fructose 1,6 bisphosphate (FBP) not only totally reversed these inhibitory effects, but also activated the enzyme to the same extent as in the absence of the inhibitors. These kinetic properties closely resemble those of vertebrate type K pyruvate kinases, and are quite distinct from those of higher vertebrate type M isozymes. Nevertheless, immunotitration studies indicate structural homology among the sturgeon, frog and dog muscle PK's as they are all precipitated by antisera to the other forms. This maintenance of structural homology, despite a marked degree of functional differentiation, suggests that only small structural modifications were required to generate the functionally specialized forms of muscle PK found among the vertebrates.</p></abstract><textClass><keywords scheme="Journal Subject"><list><head>Life Sciences</head><item><term>Biomedicine general</term></item><item><term>Human Physiology</term></item><item><term>Biochemistry, general</term></item><item><term>Zoology</term></item><item><term>Animal Physiology</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1983-06-01">Published</change><change xml:id="refBibs-istex" who="#ISTEX-API" when="2016-11-23">References added</change><change xml:id="refBibs-istex" who="#ISTEX-API" when="2017-01-21">References 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comparative physiology</JournalTitle><JournalAbbreviatedTitle>J Comp Physiol B</JournalAbbreviatedTitle><JournalSubjectGroup><JournalSubject Type="Primary">Life Sciences</JournalSubject><JournalSubject Type="Secondary">Biomedicine general</JournalSubject><JournalSubject Type="Secondary">Human Physiology</JournalSubject><JournalSubject Type="Secondary">Biochemistry, general</JournalSubject><JournalSubject Type="Secondary">Zoology</JournalSubject><JournalSubject Type="Secondary">Animal Physiology</JournalSubject></JournalSubjectGroup></JournalInfo><Volume><VolumeInfo VolumeType="Regular" TocLevels="0"><VolumeIDStart>153</VolumeIDStart><VolumeIDEnd>153</VolumeIDEnd><VolumeIssueCount>4</VolumeIssueCount></VolumeInfo><Issue IssueType="Regular"><IssueInfo TocLevels="0"><IssueIDStart>2</IssueIDStart><IssueIDEnd>2</IssueIDEnd><IssueArticleCount>15</IssueArticleCount><IssueHistory><CoverDate><DateString>1983</DateString><Year>1983</Year><Month>6</Month></CoverDate></IssueHistory><IssueCopyright><CopyrightHolderName>Springer-Verlag</CopyrightHolderName><CopyrightYear>1983</CopyrightYear></IssueCopyright></IssueInfo><Article ID="Art12"><ArticleInfo Language="En" ArticleType="OriginalPaper" NumberingStyle="Unnumbered" TocLevels="0" ContainsESM="No"><ArticleID>BF00689628</ArticleID><ArticleDOI>10.1007/BF00689628</ArticleDOI><ArticleSequenceNumber>12</ArticleSequenceNumber><ArticleTitle Language="En">Close resemblance between muscle pyruvate kinase from a primitive vertebrate, the river sturgeon<Emphasis Type="Italic">Acipenser fulvenscens</Emphasis>, and the ancestral type K isozyme</ArticleTitle><ArticleFirstPage>247</ArticleFirstPage><ArticleLastPage>256</ArticleLastPage><ArticleHistory><RegistrationDate><Year>2004</Year><Month>11</Month><Day>9</Day></RegistrationDate><Accepted><Year>1983</Year><Month>4</Month><Day>16</Day></Accepted></ArticleHistory><ArticleCopyright><CopyrightHolderName>Springer-Verlag</CopyrightHolderName><CopyrightYear>1983</CopyrightYear></ArticleCopyright><ArticleGrants Type="Regular"><MetadataGrant Grant="OpenAccess"></MetadataGrant><AbstractGrant Grant="OpenAccess"></AbstractGrant><BodyPDFGrant Grant="Restricted"></BodyPDFGrant><BodyHTMLGrant Grant="Restricted"></BodyHTMLGrant><BibliographyGrant Grant="Restricted"></BibliographyGrant><ESMGrant Grant="Restricted"></ESMGrant></ArticleGrants><ArticleContext><JournalID>359</JournalID><VolumeIDStart>153</VolumeIDStart><VolumeIDEnd>153</VolumeIDEnd><IssueIDStart>2</IssueIDStart><IssueIDEnd>2</IssueIDEnd></ArticleContext></ArticleInfo><ArticleHeader><AuthorGroup><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Helga</GivenName><FamilyName>Guderley</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Lucie</GivenName><FamilyName>Hamel</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Julie</GivenName><FamilyName>Lafond</FamilyName></AuthorName></Author><Affiliation ID="Aff1"><OrgDivision>Department de Biologie</OrgDivision><OrgName>Université Laval</OrgName><OrgAddress><Postcode>GIK 7P4</Postcode><City>Québec</City><Country>Canada</Country></OrgAddress></Affiliation></AuthorGroup><Abstract ID="Abs1" Language="En"><Heading>Summary</Heading><Para>Pyruvate kinase (PK) exists as at least two electrophoretically distinguishable, tissue specific form in the river sturgeon<Emphasis Type="Italic">Acipenser fulvenscens</Emphasis>. In contrast with the PK isozyme system in other vertebrates, the isozyme present in muscle is also present in non-musclce tissues, notably the spleen. The presence of a five membered set of hybrids in liver, gills, eyes and intestine suggests that the synthesis of this isozyme occurs in other tissues as well. Thus, in this primitive vertebrate, the specialization of one PK isozyme for function in muscle tissues is not complete. Sturgeon muscle PK had slightly cooperative phosphoenolpyruvate (PEP) saturation curves (S<Subscript>0.5</Subscript>=0.33 mM) and a Hill coefficient,<Emphasis Type="Italic">n</Emphasis><Subscript>H</Subscript>, of 1.24, and was strongly activated by fructose 1,6 bisphosphate (PEP S<Subscript>0.5</Subscript>=0.098 mM;<Emphasis Type="Italic">n</Emphasis><Subscript>H</Subscript>=1.0). The enzyme was strongly inhibited by phenylalanine, alanine and MgATP. Fructose 1,6 bisphosphate (FBP) not only totally reversed these inhibitory effects, but also activated the enzyme to the same extent as in the absence of the inhibitors. These kinetic properties closely resemble those of vertebrate type K pyruvate kinases, and are quite distinct from those of higher vertebrate type M isozymes. Nevertheless, immunotitration studies indicate structural homology among the sturgeon, frog and dog muscle PK's as they are all precipitated by antisera to the other forms. This maintenance of structural homology, despite a marked degree of functional differentiation, suggests that only small structural modifications were required to generate the functionally specialized forms of muscle PK found among the vertebrates.</Para></Abstract><AbbreviationGroup><Heading>Abbreviations</Heading><DefinitionList><DefinitionListEntry><Term><Emphasis Type="Italic">PK</Emphasis></Term><Description><Para>pyruvate kinase</Para></Description></DefinitionListEntry><DefinitionListEntry><Term><Emphasis Type="Italic">PEP</Emphasis></Term><Description><Para>phosphoenolpyruvate</Para></Description></DefinitionListEntry><DefinitionListEntry><Term><Emphasis Type="Italic">FBP</Emphasis></Term><Description><Para>fructose 1,6-bisphosphate</Para></Description></DefinitionListEntry></DefinitionList></AbbreviationGroup></ArticleHeader><NoBody></NoBody></Article></Issue></Volume></Journal></Publisher></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Close resemblance between muscle pyruvate kinase from a primitive vertebrate, the river sturgeon Acipenser fulvenscens , and the ancestral type K isozyme</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Close resemblance between muscle pyruvate kinase from a primitive vertebrate, the river sturgeonAcipenser fulvenscens, and the ancestral type K isozyme</title></titleInfo><name type="personal"><namePart type="given">Helga</namePart><namePart type="family">Guderley</namePart><affiliation>Department de Biologie, Université Laval, GIK 7P4, Québec, Canada</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Lucie</namePart><namePart type="family">Hamel</namePart><affiliation>Department de Biologie, Université Laval, GIK 7P4, Québec, Canada</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Julie</namePart><namePart type="family">Lafond</namePart><affiliation>Department de Biologie, Université Laval, GIK 7P4, Québec, Canada</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="OriginalPaper"></genre><originInfo><publisher>Springer-Verlag</publisher><place><placeTerm type="text">Berlin/Heidelberg</placeTerm></place><dateIssued encoding="w3cdtf">1983-06-01</dateIssued><copyrightDate encoding="w3cdtf">1983</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType></physicalDescription><abstract lang="en">Summary: Pyruvate kinase (PK) exists as at least two electrophoretically distinguishable, tissue specific form in the river sturgeonAcipenser fulvenscens. In contrast with the PK isozyme system in other vertebrates, the isozyme present in muscle is also present in non-musclce tissues, notably the spleen. The presence of a five membered set of hybrids in liver, gills, eyes and intestine suggests that the synthesis of this isozyme occurs in other tissues as well. Thus, in this primitive vertebrate, the specialization of one PK isozyme for function in muscle tissues is not complete. Sturgeon muscle PK had slightly cooperative phosphoenolpyruvate (PEP) saturation curves (S0.5=0.33 mM) and a Hill coefficient,n H, of 1.24, and was strongly activated by fructose 1,6 bisphosphate (PEP S0.5=0.098 mM;n H=1.0). The enzyme was strongly inhibited by phenylalanine, alanine and MgATP. Fructose 1,6 bisphosphate (FBP) not only totally reversed these inhibitory effects, but also activated the enzyme to the same extent as in the absence of the inhibitors. These kinetic properties closely resemble those of vertebrate type K pyruvate kinases, and are quite distinct from those of higher vertebrate type M isozymes. Nevertheless, immunotitration studies indicate structural homology among the sturgeon, frog and dog muscle PK's as they are all precipitated by antisera to the other forms. This maintenance of structural homology, despite a marked degree of functional differentiation, suggests that only small structural modifications were required to generate the functionally specialized forms of muscle PK found among the vertebrates.</abstract><relatedItem type="host"><titleInfo><title>Journal of comparative physiology</title></titleInfo><titleInfo type="abbreviated"><title>J Comp Physiol B</title></titleInfo><genre type="journal" displayLabel="Archive Journal"></genre><originInfo><dateIssued encoding="w3cdtf">1983-06-01</dateIssued><copyrightDate encoding="w3cdtf">1983</copyrightDate></originInfo><subject><genre>Life Sciences</genre><topic>Biomedicine general</topic><topic>Human Physiology</topic><topic>Biochemistry, general</topic><topic>Zoology</topic><topic>Animal Physiology</topic></subject><identifier type="ISSN">0340-7594</identifier><identifier type="eISSN">1432-1351</identifier><identifier type="JournalID">359</identifier><identifier type="IssueArticleCount">15</identifier><identifier type="VolumeIssueCount">4</identifier><part><date>1983</date><detail type="volume"><number>153</number><caption>vol.</caption></detail><detail type="issue"><number>2</number><caption>no.</caption></detail><extent unit="pages"><start>247</start><end>256</end></extent></part><recordInfo><recordOrigin>Springer-Verlag, 1983</recordOrigin></recordInfo></relatedItem><identifier type="istex">94802A6C84D2E1218F9C28F21BDD71DE848FA423</identifier><identifier type="DOI">10.1007/BF00689628</identifier><identifier type="ArticleID">BF00689628</identifier><identifier type="ArticleID">Art12</identifier><accessCondition type="use and reproduction" contentType="copyright">Springer-Verlag, 1983</accessCondition><recordInfo><recordContentSource>SPRINGER</recordContentSource><recordOrigin>Springer-Verlag, 1983</recordOrigin></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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{{Explor lien
|wiki= Wicri/Eau
|area= EsturgeonV1
|flux= Istex
|étape= Corpus
|type= RBID
|clé= ISTEX:94802A6C84D2E1218F9C28F21BDD71DE848FA423
|texte= Close resemblance between muscle pyruvate kinase from a primitive vertebrate, the river sturgeon Acipenser fulvenscens , and the ancestral type K isozyme
}}
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