Purification and Characterisation of a Tissue Specific Elongation Factor 1 Alpha (EF-1α2) from Rabbit Muscle
The peptide elongation factor 1 alpha (EF-1α) has been isolated and characterised from a number of species. Recently we and others have reported the existence of an isoform of the ubiquitously expressed EF-1α mRNA in higher eukaryotes, including human cells. This isoform has a tissue specific expres...
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Veröffentlicht in: | Biochemical and biophysical research communications 1998-04, Vol.245 (3), p.810-814 |
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description | The peptide elongation factor 1 alpha (EF-1α) has been isolated and characterised from a number of species. Recently we and others have reported the existence of an isoform of the ubiquitously expressed EF-1α mRNA in higher eukaryotes, including human cells. This isoform has a tissue specific expression pattern, confining it primarily to muscle, heart, and brain. In the present study we have purified the isoform of EF-1α from rabbit muscle. Using partial amino acid analysis, we can conclude that in rabbit muscle essentially only the isoform of elongation factor 1 alpha, designated EF-1α2, is translated. Preliminary activity assays show that the isoform has the same functional activities as the normal EF-1α, designated EF-1α1, in relation to protein synthesis, but may behave differently in the ability to bind nucleotides. Based on the availability of the isoforms of EF-1α purified from a mammalian species, it will be possible to conduct further comparative studies in order to elucidate the different functions of EF-1α1 and EF-1α2 proteins. |
doi_str_mv | 10.1006/bbrc.1998.8510 |
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Recently we and others have reported the existence of an isoform of the ubiquitously expressed EF-1α mRNA in higher eukaryotes, including human cells. This isoform has a tissue specific expression pattern, confining it primarily to muscle, heart, and brain. In the present study we have purified the isoform of EF-1α from rabbit muscle. Using partial amino acid analysis, we can conclude that in rabbit muscle essentially only the isoform of elongation factor 1 alpha, designated EF-1α2, is translated. Preliminary activity assays show that the isoform has the same functional activities as the normal EF-1α, designated EF-1α1, in relation to protein synthesis, but may behave differently in the ability to bind nucleotides. Based on the availability of the isoforms of EF-1α purified from a mammalian species, it will be possible to conduct further comparative studies in order to elucidate the different functions of EF-1α1 and EF-1α2 proteins.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Guanosine Diphosphate - metabolism</subject><subject>Guanosine Triphosphate - metabolism</subject><subject>Humans</subject><subject>Molecular Sequence Data</subject><subject>Muscles - chemistry</subject><subject>Peptide Elongation Factor 1</subject><subject>Peptide Elongation Factors - chemistry</subject><subject>Peptide Elongation Factors - isolation & purification</subject><subject>Rabbits</subject><subject>Sequence Alignment</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kMGK1EAQhhtR1nH16k3ok6yHjFVJJp0-LsOMCiuKruCtqXSq3ZYkPXYngo_li_hMJmTY254K6v_qh_qEeImwRYDqbdNEu0Wt6229Q3gkNggashyhfCw2MBNZrvH7U_EspZ8AiGWlL8SF3tU16moj-s9T9M5bGn0YJA2t3N9RJDty9GldBidJ3vqUJpZfT2wXXB66MPxY8-NMhyhRXnenO5JXh2OG__7mb6SLoZdfqGn8KD9OyXb8XDxx1CV-cZ6X4tvxcLt_n918evdhf32T2aLQY4as61o1WpVYFk7V-c62ruLWaleCzYGI0KlK7QiYQKlWU9kUlrQDzpu8LC7F67X3FMOvidNoep8sdx0NHKZk1NwPSuMMblfQxpBSZGdO0fcU_xgEs_g1i1-z-DWL3_ng1bl5anpu7_Gz0Dmv15zn9357jiZZz4Pl1ke2o2mDf6j6PzUjihc</recordid><startdate>19980428</startdate><enddate>19980428</enddate><creator>Kristensen, Peter</creator><creator>Lund, Ann</creator><creator>Clark, Brian F.C.</creator><creator>Cavallius, Jens</creator><creator>Merrick, William C.</creator><general>Elsevier Inc</general><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>19980428</creationdate><title>Purification and Characterisation of a Tissue Specific Elongation Factor 1 Alpha (EF-1α2) from Rabbit Muscle</title><author>Kristensen, Peter ; Lund, Ann ; Clark, Brian F.C. ; Cavallius, Jens ; Merrick, William C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c339t-1e9887b974143f7825cdf6edc9f40c20aaa1f7675a0ea077d9a4b3ca9f0e2b243</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Guanosine Diphosphate - metabolism</topic><topic>Guanosine Triphosphate - metabolism</topic><topic>Humans</topic><topic>Molecular Sequence Data</topic><topic>Muscles - chemistry</topic><topic>Peptide Elongation Factor 1</topic><topic>Peptide Elongation Factors - chemistry</topic><topic>Peptide Elongation Factors - isolation & purification</topic><topic>Rabbits</topic><topic>Sequence Alignment</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kristensen, Peter</creatorcontrib><creatorcontrib>Lund, Ann</creatorcontrib><creatorcontrib>Clark, Brian F.C.</creatorcontrib><creatorcontrib>Cavallius, Jens</creatorcontrib><creatorcontrib>Merrick, William C.</creatorcontrib><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>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kristensen, Peter</au><au>Lund, Ann</au><au>Clark, Brian F.C.</au><au>Cavallius, Jens</au><au>Merrick, William C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and Characterisation of a Tissue Specific Elongation Factor 1 Alpha (EF-1α2) from Rabbit Muscle</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1998-04-28</date><risdate>1998</risdate><volume>245</volume><issue>3</issue><spage>810</spage><epage>814</epage><pages>810-814</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>The peptide elongation factor 1 alpha (EF-1α) has been isolated and characterised from a number of species. Recently we and others have reported the existence of an isoform of the ubiquitously expressed EF-1α mRNA in higher eukaryotes, including human cells. This isoform has a tissue specific expression pattern, confining it primarily to muscle, heart, and brain. In the present study we have purified the isoform of EF-1α from rabbit muscle. Using partial amino acid analysis, we can conclude that in rabbit muscle essentially only the isoform of elongation factor 1 alpha, designated EF-1α2, is translated. Preliminary activity assays show that the isoform has the same functional activities as the normal EF-1α, designated EF-1α1, in relation to protein synthesis, but may behave differently in the ability to bind nucleotides. Based on the availability of the isoforms of EF-1α purified from a mammalian species, it will be possible to conduct further comparative studies in order to elucidate the different functions of EF-1α1 and EF-1α2 proteins.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>9588196</pmid><doi>10.1006/bbrc.1998.8510</doi><tpages>5</tpages></addata></record> |
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subjects | Amino Acid Sequence Animals Electrophoresis, Polyacrylamide Gel Guanosine Diphosphate - metabolism Guanosine Triphosphate - metabolism Humans Molecular Sequence Data Muscles - chemistry Peptide Elongation Factor 1 Peptide Elongation Factors - chemistry Peptide Elongation Factors - isolation & purification Rabbits Sequence Alignment |
title | Purification and Characterisation of a Tissue Specific Elongation Factor 1 Alpha (EF-1α2) from Rabbit Muscle |
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