Developmental changes in the pyruvate kinase isozymes of coho salmon
Identifieur interne : 000F44 ( Istex/Corpus ); précédent : 000F43; suivant : 000F45Developmental changes in the pyruvate kinase isozymes of coho salmon
Auteurs : Helga E. Guderley ; Janet M. CardenasSource :
- Journal of Experimental Zoology [ 0022-104X ] ; 1979-04.
Abstract
Pyruvate kinase exists as two major isozymes in coho salmon. As in mammals and birds, one form is present in the early embryo and maintains a wide tissue distribution in adults. This salmonid type K shows anodal migration during electrophoresis at pH 7.5. The appearance of the second major pyruvate kinase isozyme coincides with the appearance of functional musculature in the developing embryos. In adult animals this second form is the only pyruvate kinase in muscle. Brain, kidney, liver and gill contain primarily the type K pyruvate kinase while heart contains both major forms along with three intermediate forms which presumably constitute a hybrid set. Since there is no additional isozyme restricted to gluconeogenic tissues, we conclude that a type L isozyme has not developed in these animals. The two major isozymes are immunologically distinct. Both forms are subject to fructose 1,6‐bisphosphate activation of phosphoenolpyruvate binding, but the magnitude of the effect is small. The affinities for phosphoenolpyruvate are similar, but salmon type K has hyperbolic saturation curves with this substrate and type M has sigmoidal saturation curves. While the immunological data indicates considerable divergence in structure, the kinetic parameters of the two forms have remained relatively similar.
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DOI: 10.1002/jez.1402080102
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Guderley</name><affiliation><mods:affiliation>Department of Biochemistry and Biophysics, Oregon State University, Corvallis, Oregon 97331</mods:affiliation></affiliation></author><author><name sortKey="Cardenas, Janet M" sort="Cardenas, Janet M" uniqKey="Cardenas J" first="Janet M." last="Cardenas">Janet M. Cardenas</name><affiliation><mods:affiliation>Department of Biochemistry and Biophysics, Oregon State University, Corvallis, Oregon 97331</mods:affiliation></affiliation><affiliation><mods:affiliation>Current Address: Department of Chemistry, University of North Carolina, Chapel Hill, North Carolina 27514</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Journal of Experimental Zoology</title><title level="j" type="abbrev">J. Exp. 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As in mammals and birds, one form is present in the early embryo and maintains a wide tissue distribution in adults. This salmonid type K shows anodal migration during electrophoresis at pH 7.5. The appearance of the second major pyruvate kinase isozyme coincides with the appearance of functional musculature in the developing embryos. In adult animals this second form is the only pyruvate kinase in muscle. Brain, kidney, liver and gill contain primarily the type K pyruvate kinase while heart contains both major forms along with three intermediate forms which presumably constitute a hybrid set. Since there is no additional isozyme restricted to gluconeogenic tissues, we conclude that a type L isozyme has not developed in these animals. The two major isozymes are immunologically distinct. Both forms are subject to fructose 1,6‐bisphosphate activation of phosphoenolpyruvate binding, but the magnitude of the effect is small. The affinities for phosphoenolpyruvate are similar, but salmon type K has hyperbolic saturation curves with this substrate and type M has sigmoidal saturation curves. While the immunological data indicates considerable divergence in structure, the kinetic parameters of the two forms have remained relatively similar.</div></front></TEI><istex><corpusName>wiley</corpusName><author><json:item><name>Helga E. Guderley</name><affiliations><json:string>Department of Biochemistry and Biophysics, Oregon State University, Corvallis, Oregon 97331</json:string></affiliations></json:item><json:item><name>Janet M. Cardenas</name><affiliations><json:string>Department of Biochemistry and Biophysics, Oregon State University, Corvallis, Oregon 97331</json:string><json:string>Current Address: Department of Chemistry, University of North Carolina, Chapel Hill, North Carolina 27514</json:string></affiliations></json:item></author><articleId><json:string>JEZ1402080102</json:string></articleId><language><json:string>eng</json:string></language><originalGenre><json:string>article</json:string></originalGenre><abstract>Pyruvate kinase exists as two major isozymes in coho salmon. As in mammals and birds, one form is present in the early embryo and maintains a wide tissue distribution in adults. This salmonid type K shows anodal migration during electrophoresis at pH 7.5. The appearance of the second major pyruvate kinase isozyme coincides with the appearance of functional musculature in the developing embryos. In adult animals this second form is the only pyruvate kinase in muscle. Brain, kidney, liver and gill contain primarily the type K pyruvate kinase while heart contains both major forms along with three intermediate forms which presumably constitute a hybrid set. Since there is no additional isozyme restricted to gluconeogenic tissues, we conclude that a type L isozyme has not developed in these animals. The two major isozymes are immunologically distinct. Both forms are subject to fructose 1,6‐bisphosphate activation of phosphoenolpyruvate binding, but the magnitude of the effect is small. The affinities for phosphoenolpyruvate are similar, but salmon type K has hyperbolic saturation curves with this substrate and type M has sigmoidal saturation curves. 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Exp. Zool.</title><idno type="pISSN">0022-104X</idno><idno type="eISSN">1097-010X</idno><idno type="DOI">10.1002/(ISSN)1097-010X</idno><imprint><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>New York</pubPlace><date type="published" when="1979-04"></date><biblScope unit="volume">208</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="1">1</biblScope><biblScope unit="page" to="12">12</biblScope></imprint></monogr><idno type="istex">C76FC1060A2A60BEB95AB8B5F132D03A2CC74787</idno><idno type="DOI">10.1002/jez.1402080102</idno><idno type="ArticleID">JEZ1402080102</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1979</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Pyruvate kinase exists as two major isozymes in coho salmon. As in mammals and birds, one form is present in the early embryo and maintains a wide tissue distribution in adults. This salmonid type K shows anodal migration during electrophoresis at pH 7.5. The appearance of the second major pyruvate kinase isozyme coincides with the appearance of functional musculature in the developing embryos. In adult animals this second form is the only pyruvate kinase in muscle. Brain, kidney, liver and gill contain primarily the type K pyruvate kinase while heart contains both major forms along with three intermediate forms which presumably constitute a hybrid set. Since there is no additional isozyme restricted to gluconeogenic tissues, we conclude that a type L isozyme has not developed in these animals. The two major isozymes are immunologically distinct. Both forms are subject to fructose 1,6‐bisphosphate activation of phosphoenolpyruvate binding, but the magnitude of the effect is small. The affinities for phosphoenolpyruvate are similar, but salmon type K has hyperbolic saturation curves with this substrate and type M has sigmoidal saturation curves. 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As in mammals and birds, one form is present in the early embryo and maintains a wide tissue distribution in adults. This salmonid type K shows anodal migration during electrophoresis at pH 7.5. The appearance of the second major pyruvate kinase isozyme coincides with the appearance of functional musculature in the developing embryos. In adult animals this second form is the only pyruvate kinase in muscle. Brain, kidney, liver and gill contain primarily the type K pyruvate kinase while heart contains both major forms along with three intermediate forms which presumably constitute a hybrid set. Since there is no additional isozyme restricted to gluconeogenic tissues, we conclude that a type L isozyme has not developed in these animals.</p><p>The two major isozymes are immunologically distinct. Both forms are subject to fructose 1,6‐bisphosphate activation of phosphoenolpyruvate binding, but the magnitude of the effect is small. The affinities for phosphoenolpyruvate are similar, but salmon type K has hyperbolic saturation curves with this substrate and type M has sigmoidal saturation curves. While the immunological data indicates considerable divergence in structure, the kinetic parameters of the two forms have remained relatively similar.</p></abstract></abstractGroup></contentMeta><noteGroup><note xml:id="fn1"><p>A preliminary report of this work was presented at the 1978 meeting of the American Society of Biological Chemists, Atlanta, Georgia, June 4–8.</p></note></noteGroup></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Developmental changes in the pyruvate kinase isozymes of coho salmon</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>PYRUVATE KINASE ISOZYMES OF SALMON</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Developmental changes in the pyruvate kinase isozymes of coho salmon</title></titleInfo><name type="personal"><namePart type="given">Helga E.</namePart><namePart type="family">Guderley</namePart><affiliation>Department of Biochemistry and Biophysics, Oregon State University, Corvallis, Oregon 97331</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Janet M.</namePart><namePart type="family">Cardenas</namePart><affiliation>Department of Biochemistry and Biophysics, Oregon State University, Corvallis, Oregon 97331</affiliation><affiliation>Current Address: Department of Chemistry, University of North Carolina, Chapel Hill, North Carolina 27514</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article"></genre><originInfo><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><place><placeTerm type="text">New York</placeTerm></place><dateIssued encoding="w3cdtf">1979-04</dateIssued><copyrightDate encoding="w3cdtf">1979</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType><extent unit="figures">7</extent><extent unit="tables">2</extent><extent unit="references">47</extent></physicalDescription><abstract lang="en">Pyruvate kinase exists as two major isozymes in coho salmon. As in mammals and birds, one form is present in the early embryo and maintains a wide tissue distribution in adults. This salmonid type K shows anodal migration during electrophoresis at pH 7.5. The appearance of the second major pyruvate kinase isozyme coincides with the appearance of functional musculature in the developing embryos. In adult animals this second form is the only pyruvate kinase in muscle. Brain, kidney, liver and gill contain primarily the type K pyruvate kinase while heart contains both major forms along with three intermediate forms which presumably constitute a hybrid set. Since there is no additional isozyme restricted to gluconeogenic tissues, we conclude that a type L isozyme has not developed in these animals. The two major isozymes are immunologically distinct. Both forms are subject to fructose 1,6‐bisphosphate activation of phosphoenolpyruvate binding, but the magnitude of the effect is small. The affinities for phosphoenolpyruvate are similar, but salmon type K has hyperbolic saturation curves with this substrate and type M has sigmoidal saturation curves. While the immunological data indicates considerable divergence in structure, the kinetic parameters of the two forms have remained relatively similar.</abstract><note type="content">*A preliminary report of this work was presented at the 1978 meeting of the American Society of Biological Chemists, Atlanta, Georgia, June 4–8.</note><note type="funding">NIH - No. AM-15645; </note><note type="funding">Research Career Development Award - No. AM-00191; </note><relatedItem type="host"><titleInfo><title>Journal of Experimental Zoology</title></titleInfo><titleInfo type="abbreviated"><title>J. Exp. 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