Refolding kinetics of pig muscle and yeast 3-phosphoglycerate kinases and of their proteolytic fragments
The time course of refolding of both pig muscle and yeast 3-phosphoglycerate kinase (molecular masses about 47 kDa), as well as their proteolytic C-terminal fragments (30 and 33 kDa, respectively) has been investigated. Very similar refolding kinetics (with half-time between 80-120 s, at 20 degrees...
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| Veröffentlicht in: | European journal of biochemistry 1991-12, Vol.202 (3), p.1083-1089 |
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| container_title | European journal of biochemistry |
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| creator | SEMISOTNOV, Gennady V. VAS, Maria CHEMERIS, Violetta V. KASHPAROVA, Natalija J. KOTOVA, Nina V. RAZGULYAEV, Oleg I. SINEV, Michael A. |
| description | The time course of refolding of both pig muscle and yeast 3-phosphoglycerate kinase (molecular masses about 47 kDa), as well as their proteolytic C-terminal fragments (30 and 33 kDa, respectively) has been investigated. Very similar refolding kinetics (with half-time between 80-120 s, at 20 degrees C) were observed by fluorescence and ultraviolet absorbance spectroscopy, as well as by activity measurements, for the intact enzyme from both sources. This time course appears not to depend on the time the protein spends in the unfolded state, i.e. it is certainly not controlled by proline isomerization. Furthermore, after removal of a large N-terminal part (molecular mass of about 18 kDa for pig muscle enzyme or 13 kDa for yeast enzyme) of the molecule by proteolysis, refolding of the remaining C-terminal fragment of both proteins follows kinetics virtually indistinguishable from those of the intact protein molecule. |
| doi_str_mv | 10.1111/j.1432-1033.1991.tb16474.x |
| format | Article |
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Very similar refolding kinetics (with half-time between 80-120 s, at 20 degrees C) were observed by fluorescence and ultraviolet absorbance spectroscopy, as well as by activity measurements, for the intact enzyme from both sources. This time course appears not to depend on the time the protein spends in the unfolded state, i.e. it is certainly not controlled by proline isomerization. Furthermore, after removal of a large N-terminal part (molecular mass of about 18 kDa for pig muscle enzyme or 13 kDa for yeast enzyme) of the molecule by proteolysis, refolding of the remaining C-terminal fragment of both proteins follows kinetics virtually indistinguishable from those of the intact protein molecule.</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>DOI: 10.1111/j.1432-1033.1991.tb16474.x</identifier><identifier>PMID: 1765069</identifier><identifier>CODEN: EJBCAI</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Amino Acid Sequence ; animal physiology ; Animals ; Biological and medical sciences ; Calorimetry ; cerdo ; Conformational dynamics in molecular biology ; fisiologia animal ; Fundamental and applied biological sciences. Psychology ; isomerisation ; isomerizacion ; isomerization ; Kinetics ; levadura ; levure ; Molecular biophysics ; Molecular Sequence Data ; Molecular Weight ; muscle ; muscles ; Muscles - enzymology ; musculos ; Peptide Fragments - chemistry ; Peptide Fragments - metabolism ; Phosphoglycerate Kinase - chemistry ; Phosphoglycerate Kinase - metabolism ; physiologie animale ; porcin ; prolina ; proline ; Protein Conformation ; Protein Denaturation ; proteolisis ; proteolyse ; proteolysis ; Saccharomyces cerevisiae - enzymology ; Spectrometry, Fluorescence ; Spectrophotometry, Ultraviolet ; Swine ; Time Factors ; transferasas ; transferase ; transferases ; yeasts</subject><ispartof>European journal of biochemistry, 1991-12, Vol.202 (3), p.1083-1089</ispartof><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4753-31cd09013280b1e52ac671532495d94cbb3a183f8b1e723615046effe258ae213</citedby><cites>FETCH-LOGICAL-c4753-31cd09013280b1e52ac671532495d94cbb3a183f8b1e723615046effe258ae213</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5030546$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1765069$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>SEMISOTNOV, Gennady V.</creatorcontrib><creatorcontrib>VAS, Maria</creatorcontrib><creatorcontrib>CHEMERIS, Violetta V.</creatorcontrib><creatorcontrib>KASHPAROVA, Natalija J.</creatorcontrib><creatorcontrib>KOTOVA, Nina V.</creatorcontrib><creatorcontrib>RAZGULYAEV, Oleg I.</creatorcontrib><creatorcontrib>SINEV, Michael A.</creatorcontrib><creatorcontrib>USSR Academy of Sciences, Pushchino, USSR</creatorcontrib><title>Refolding kinetics of pig muscle and yeast 3-phosphoglycerate kinases and of their proteolytic fragments</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>The time course of refolding of both pig muscle and yeast 3-phosphoglycerate kinase (molecular masses about 47 kDa), as well as their proteolytic C-terminal fragments (30 and 33 kDa, respectively) has been investigated. Very similar refolding kinetics (with half-time between 80-120 s, at 20 degrees C) were observed by fluorescence and ultraviolet absorbance spectroscopy, as well as by activity measurements, for the intact enzyme from both sources. This time course appears not to depend on the time the protein spends in the unfolded state, i.e. it is certainly not controlled by proline isomerization. Furthermore, after removal of a large N-terminal part (molecular mass of about 18 kDa for pig muscle enzyme or 13 kDa for yeast enzyme) of the molecule by proteolysis, refolding of the remaining C-terminal fragment of both proteins follows kinetics virtually indistinguishable from those of the intact protein molecule.</description><subject>Amino Acid Sequence</subject><subject>animal physiology</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Calorimetry</subject><subject>cerdo</subject><subject>Conformational dynamics in molecular biology</subject><subject>fisiologia animal</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>isomerisation</subject><subject>isomerizacion</subject><subject>isomerization</subject><subject>Kinetics</subject><subject>levadura</subject><subject>levure</subject><subject>Molecular biophysics</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>muscle</subject><subject>muscles</subject><subject>Muscles - enzymology</subject><subject>musculos</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - metabolism</subject><subject>Phosphoglycerate Kinase - chemistry</subject><subject>Phosphoglycerate Kinase - metabolism</subject><subject>physiologie animale</subject><subject>porcin</subject><subject>prolina</subject><subject>proline</subject><subject>Protein Conformation</subject><subject>Protein Denaturation</subject><subject>proteolisis</subject><subject>proteolyse</subject><subject>proteolysis</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Spectrometry, Fluorescence</subject><subject>Spectrophotometry, Ultraviolet</subject><subject>Swine</subject><subject>Time Factors</subject><subject>transferasas</subject><subject>transferase</subject><subject>transferases</subject><subject>yeasts</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkEtv1DAUhS1EVaaFnwCyEOouqW_8SMIKqFpaqRISpWvLcW4yHvIY7Ixo_j0OGZU1li1bOt851zqEvAeWQlyXuxQEzxJgnKdQlpBOFSiRi_TpBdk8Sy_JhjEQSVZK9YqchbBjjKlS5afkFHIl43tDtt-xGbvaDS396QacnA10bOjetbQ_BNshNUNNZzRhojzZb8cQT9vNFr2ZcPGYgOEvFG3TFp2nez9OOHZzDKONN22PwxRek5PGdAHfHO9z8nhz_ePqNrn_9vXu6vN9YkUuecLB1qxkwLOCVYAyM1blIHkmSlmXwlYVN1DwpohinnEFkgmFTYOZLAxmwM_JxZobf_HrgGHSvQsWu84MOB6CziNYcraAH1fQ-jEEj43ee9cbP2tgeqlZ7_TSpV661EvN-lizformt8cph6rH-p917TXqH466CdZ0sYXBuvCMScaZFCpin1bst-tw_o8P6JvrLw_ACh4j3q0RjRm1aX2c8vgQ4YyxPI-b_wFW5qOG</recordid><startdate>19911218</startdate><enddate>19911218</enddate><creator>SEMISOTNOV, Gennady V.</creator><creator>VAS, Maria</creator><creator>CHEMERIS, Violetta V.</creator><creator>KASHPAROVA, Natalija J.</creator><creator>KOTOVA, Nina V.</creator><creator>RAZGULYAEV, Oleg I.</creator><creator>SINEV, Michael A.</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</general><scope>FBQ</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19911218</creationdate><title>Refolding kinetics of pig muscle and yeast 3-phosphoglycerate kinases and of their proteolytic fragments</title><author>SEMISOTNOV, Gennady V. ; VAS, Maria ; CHEMERIS, Violetta V. ; KASHPAROVA, Natalija J. ; KOTOVA, Nina V. ; RAZGULYAEV, Oleg I. ; SINEV, Michael A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4753-31cd09013280b1e52ac671532495d94cbb3a183f8b1e723615046effe258ae213</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Amino Acid Sequence</topic><topic>animal physiology</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Calorimetry</topic><topic>cerdo</topic><topic>Conformational dynamics in molecular biology</topic><topic>fisiologia animal</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>isomerisation</topic><topic>isomerizacion</topic><topic>isomerization</topic><topic>Kinetics</topic><topic>levadura</topic><topic>levure</topic><topic>Molecular biophysics</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>muscle</topic><topic>muscles</topic><topic>Muscles - enzymology</topic><topic>musculos</topic><topic>Peptide Fragments - chemistry</topic><topic>Peptide Fragments - metabolism</topic><topic>Phosphoglycerate Kinase - chemistry</topic><topic>Phosphoglycerate Kinase - metabolism</topic><topic>physiologie animale</topic><topic>porcin</topic><topic>prolina</topic><topic>proline</topic><topic>Protein Conformation</topic><topic>Protein Denaturation</topic><topic>proteolisis</topic><topic>proteolyse</topic><topic>proteolysis</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Spectrometry, Fluorescence</topic><topic>Spectrophotometry, Ultraviolet</topic><topic>Swine</topic><topic>Time Factors</topic><topic>transferasas</topic><topic>transferase</topic><topic>transferases</topic><topic>yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>SEMISOTNOV, Gennady V.</creatorcontrib><creatorcontrib>VAS, Maria</creatorcontrib><creatorcontrib>CHEMERIS, Violetta V.</creatorcontrib><creatorcontrib>KASHPAROVA, Natalija J.</creatorcontrib><creatorcontrib>KOTOVA, Nina V.</creatorcontrib><creatorcontrib>RAZGULYAEV, Oleg I.</creatorcontrib><creatorcontrib>SINEV, Michael A.</creatorcontrib><creatorcontrib>USSR Academy of Sciences, Pushchino, USSR</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>SEMISOTNOV, Gennady V.</au><au>VAS, Maria</au><au>CHEMERIS, Violetta V.</au><au>KASHPAROVA, Natalija J.</au><au>KOTOVA, Nina V.</au><au>RAZGULYAEV, Oleg I.</au><au>SINEV, Michael A.</au><aucorp>USSR Academy of Sciences, Pushchino, USSR</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Refolding kinetics of pig muscle and yeast 3-phosphoglycerate kinases and of their proteolytic fragments</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1991-12-18</date><risdate>1991</risdate><volume>202</volume><issue>3</issue><spage>1083</spage><epage>1089</epage><pages>1083-1089</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><coden>EJBCAI</coden><abstract>The time course of refolding of both pig muscle and yeast 3-phosphoglycerate kinase (molecular masses about 47 kDa), as well as their proteolytic C-terminal fragments (30 and 33 kDa, respectively) has been investigated. Very similar refolding kinetics (with half-time between 80-120 s, at 20 degrees C) were observed by fluorescence and ultraviolet absorbance spectroscopy, as well as by activity measurements, for the intact enzyme from both sources. This time course appears not to depend on the time the protein spends in the unfolded state, i.e. it is certainly not controlled by proline isomerization. Furthermore, after removal of a large N-terminal part (molecular mass of about 18 kDa for pig muscle enzyme or 13 kDa for yeast enzyme) of the molecule by proteolysis, refolding of the remaining C-terminal fragment of both proteins follows kinetics virtually indistinguishable from those of the intact protein molecule.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>1765069</pmid><doi>10.1111/j.1432-1033.1991.tb16474.x</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence animal physiology Animals Biological and medical sciences Calorimetry cerdo Conformational dynamics in molecular biology fisiologia animal Fundamental and applied biological sciences. Psychology isomerisation isomerizacion isomerization Kinetics levadura levure Molecular biophysics Molecular Sequence Data Molecular Weight muscle muscles Muscles - enzymology musculos Peptide Fragments - chemistry Peptide Fragments - metabolism Phosphoglycerate Kinase - chemistry Phosphoglycerate Kinase - metabolism physiologie animale porcin prolina proline Protein Conformation Protein Denaturation proteolisis proteolyse proteolysis Saccharomyces cerevisiae - enzymology Spectrometry, Fluorescence Spectrophotometry, Ultraviolet Swine Time Factors transferasas transferase transferases yeasts |
| title | Refolding kinetics of pig muscle and yeast 3-phosphoglycerate kinases and of their proteolytic fragments |
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