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...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Biochemical and biophysical research communications 1998-04, Vol.245 (3), p.810-814
Hauptverfasser: Kristensen, Peter, Lund, Ann, Clark, Brian F.C., Cavallius, Jens, Merrick, William C.
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 814
container_issue 3
container_start_page 810
container_title Biochemical and biophysical research communications
container_volume 245
creator Kristensen, Peter
Lund, Ann
Clark, Brian F.C.
Cavallius, Jens
Merrick, William C.
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
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_79880791</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0006291X98985102</els_id><sourcerecordid>79880791</sourcerecordid><originalsourceid>FETCH-LOGICAL-c339t-1e9887b974143f7825cdf6edc9f40c20aaa1f7675a0ea077d9a4b3ca9f0e2b243</originalsourceid><addsrcrecordid>eNp1kMGK1EAQhhtR1nH16k3ok6yHjFVJJp0-LsOMCiuKruCtqXSq3ZYkPXYngo_li_hMJmTY254K6v_qh_qEeImwRYDqbdNEu0Wt6229Q3gkNggashyhfCw2MBNZrvH7U_EspZ8AiGWlL8SF3tU16moj-s9T9M5bGn0YJA2t3N9RJDty9GldBidJ3vqUJpZfT2wXXB66MPxY8-NMhyhRXnenO5JXh2OG__7mb6SLoZdfqGn8KD9OyXb8XDxx1CV-cZ6X4tvxcLt_n918evdhf32T2aLQY4as61o1WpVYFk7V-c62ruLWaleCzYGI0KlK7QiYQKlWU9kUlrQDzpu8LC7F67X3FMOvidNoep8sdx0NHKZk1NwPSuMMblfQxpBSZGdO0fcU_xgEs_g1i1-z-DWL3_ng1bl5anpu7_Gz0Dmv15zn9357jiZZz4Pl1ke2o2mDf6j6PzUjihc</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>79880791</pqid></control><display><type>article</type><title>Purification and Characterisation of a Tissue Specific Elongation Factor 1 Alpha (EF-1α2) from Rabbit Muscle</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Kristensen, Peter ; Lund, Ann ; Clark, Brian F.C. ; Cavallius, Jens ; Merrick, William C.</creator><creatorcontrib>Kristensen, Peter ; Lund, Ann ; Clark, Brian F.C. ; Cavallius, Jens ; Merrick, William C.</creatorcontrib><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.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1006/bbrc.1998.8510</identifier><identifier>PMID: 9588196</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>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 &amp; purification ; Rabbits ; Sequence Alignment</subject><ispartof>Biochemical and biophysical research communications, 1998-04, Vol.245 (3), p.810-814</ispartof><rights>1998 Academic Press</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c339t-1e9887b974143f7825cdf6edc9f40c20aaa1f7675a0ea077d9a4b3ca9f0e2b243</citedby><cites>FETCH-LOGICAL-c339t-1e9887b974143f7825cdf6edc9f40c20aaa1f7675a0ea077d9a4b3ca9f0e2b243</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006291X98985102$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9588196$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kristensen, Peter</creatorcontrib><creatorcontrib>Lund, Ann</creatorcontrib><creatorcontrib>Clark, Brian F.C.</creatorcontrib><creatorcontrib>Cavallius, Jens</creatorcontrib><creatorcontrib>Merrick, William C.</creatorcontrib><title>Purification and Characterisation of a Tissue Specific Elongation Factor 1 Alpha (EF-1α2) from Rabbit Muscle</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><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.</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 &amp; 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 &amp; 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>
fulltext fulltext
identifier ISSN: 0006-291X
ispartof Biochemical and biophysical research communications, 1998-04, Vol.245 (3), p.810-814
issn 0006-291X
1090-2104
language eng
recordid cdi_proquest_miscellaneous_79880791
source MEDLINE; Elsevier ScienceDirect Journals
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
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-25T08%3A24%3A25IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Purification%20and%20Characterisation%20of%20a%20Tissue%20Specific%20Elongation%20Factor%201%20Alpha%20(EF-1%CE%B12)%20from%20Rabbit%20Muscle&rft.jtitle=Biochemical%20and%20biophysical%20research%20communications&rft.au=Kristensen,%20Peter&rft.date=1998-04-28&rft.volume=245&rft.issue=3&rft.spage=810&rft.epage=814&rft.pages=810-814&rft.issn=0006-291X&rft.eissn=1090-2104&rft_id=info:doi/10.1006/bbrc.1998.8510&rft_dat=%3Cproquest_cross%3E79880791%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=79880791&rft_id=info:pmid/9588196&rft_els_id=S0006291X98985102&rfr_iscdi=true