Biochemical properties of C78SC96S rhFGF-2: A double point-mutated rhFGF-2 increases obviously its activity
Fibroblast growth factor-2 (FGF-2) is a multifunctional polypeptide that affects many cellular functions and phenomena. The wild-type recombinant human fibroblast growth factor rhFGF-2 W and the mutant C78SC96S rhFGF-2 M were expressed in Escherichia coli and their products were purified. The result...
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| Veröffentlicht in: | Journal of biotechnology 2006-02, Vol.121 (4), p.442-447 |
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| container_issue | 4 |
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| container_title | Journal of biotechnology |
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| creator | Wang, Ju Hong, An Ren, Jin-song Sun, Fen-Yong Shi, Ying-jiao Liu, Kan Xie, Qiu-Ling Dai, Yun Li, Zhi-ying Chen, Yu |
| description | Fibroblast growth factor-2 (FGF-2) is a multifunctional polypeptide that affects many cellular functions and phenomena. The wild-type recombinant human fibroblast growth factor rhFGF-2
W and the mutant C78SC96S rhFGF-2
M were expressed in
Escherichia coli and their products were purified. The results by the means of fluorescence spectroscopy and CD spectrums, suggested that due to its decreased hydrophobicity rhFGF-2 is not deposited as an inclusion body. The mitogenic activity of the expressed rhFGF-2
M on 3T3 fibroblasts was shown to be 10-fold more than the expressed rhFGF-2
W of which the biological activity was a little less than that of the standard rhbFGF
W, indicating that the increased biological activity was due to the change of its secondary structure, dimerization and affinity binding to FGF receptor (FGFR). |
| doi_str_mv | 10.1016/j.jbiotec.2005.08.021 |
| format | Article |
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W and the mutant C78SC96S rhFGF-2
M were expressed in
Escherichia coli and their products were purified. The results by the means of fluorescence spectroscopy and CD spectrums, suggested that due to its decreased hydrophobicity rhFGF-2 is not deposited as an inclusion body. The mitogenic activity of the expressed rhFGF-2
M on 3T3 fibroblasts was shown to be 10-fold more than the expressed rhFGF-2
W of which the biological activity was a little less than that of the standard rhbFGF
W, indicating that the increased biological activity was due to the change of its secondary structure, dimerization and affinity binding to FGF receptor (FGFR).</description><identifier>ISSN: 0168-1656</identifier><identifier>EISSN: 1873-4863</identifier><identifier>DOI: 10.1016/j.jbiotec.2005.08.021</identifier><identifier>PMID: 16223539</identifier><identifier>CODEN: JBITD4</identifier><language>eng</language><publisher>Lausanne: Elsevier B.V</publisher><subject>3T3 Cells ; Amino Acid Substitution ; Animals ; Biological and medical sciences ; Biotechnology ; Cell Proliferation - drug effects ; Escherichia coli ; Fibroblast Growth Factor 2 - chemistry ; Fibroblast Growth Factor 2 - genetics ; Fibroblast Growth Factor 2 - pharmacology ; Fluorescence spectroscopy ; Fundamental and applied biological sciences. Psychology ; Humans ; Mice ; Mitogenic activity ; Mutation ; Point Mutation ; Protein Structure, Secondary - genetics ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - pharmacology ; rhFGF-2 ; Structure-Activity Relationship</subject><ispartof>Journal of biotechnology, 2006-02, Vol.121 (4), p.442-447</ispartof><rights>2005</rights><rights>2006 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c424t-52a1835c6b152aa132cce6e071c982d71764c036026538375a57850ae823fe163</citedby><cites>FETCH-LOGICAL-c424t-52a1835c6b152aa132cce6e071c982d71764c036026538375a57850ae823fe163</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.jbiotec.2005.08.021$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,781,785,3551,27928,27929,45999</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17556711$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16223539$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Ju</creatorcontrib><creatorcontrib>Hong, An</creatorcontrib><creatorcontrib>Ren, Jin-song</creatorcontrib><creatorcontrib>Sun, Fen-Yong</creatorcontrib><creatorcontrib>Shi, Ying-jiao</creatorcontrib><creatorcontrib>Liu, Kan</creatorcontrib><creatorcontrib>Xie, Qiu-Ling</creatorcontrib><creatorcontrib>Dai, Yun</creatorcontrib><creatorcontrib>Li, Zhi-ying</creatorcontrib><creatorcontrib>Chen, Yu</creatorcontrib><title>Biochemical properties of C78SC96S rhFGF-2: A double point-mutated rhFGF-2 increases obviously its activity</title><title>Journal of biotechnology</title><addtitle>J Biotechnol</addtitle><description>Fibroblast growth factor-2 (FGF-2) is a multifunctional polypeptide that affects many cellular functions and phenomena. The wild-type recombinant human fibroblast growth factor rhFGF-2
W and the mutant C78SC96S rhFGF-2
M were expressed in
Escherichia coli and their products were purified. The results by the means of fluorescence spectroscopy and CD spectrums, suggested that due to its decreased hydrophobicity rhFGF-2 is not deposited as an inclusion body. The mitogenic activity of the expressed rhFGF-2
M on 3T3 fibroblasts was shown to be 10-fold more than the expressed rhFGF-2
W of which the biological activity was a little less than that of the standard rhbFGF
W, indicating that the increased biological activity was due to the change of its secondary structure, dimerization and affinity binding to FGF receptor (FGFR).</description><subject>3T3 Cells</subject><subject>Amino Acid Substitution</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Cell Proliferation - drug effects</subject><subject>Escherichia coli</subject><subject>Fibroblast Growth Factor 2 - chemistry</subject><subject>Fibroblast Growth Factor 2 - genetics</subject><subject>Fibroblast Growth Factor 2 - pharmacology</subject><subject>Fluorescence spectroscopy</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Mice</subject><subject>Mitogenic activity</subject><subject>Mutation</subject><subject>Point Mutation</subject><subject>Protein Structure, Secondary - genetics</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - pharmacology</subject><subject>rhFGF-2</subject><subject>Structure-Activity Relationship</subject><issn>0168-1656</issn><issn>1873-4863</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1v1DAQhi0EokvhJ4B8gVuCP-KPcEHtii1IlTgUzpbjTFQvSbzYzkr77_Fqg3rsyZb8vOOZeRB6T0lNCZWf9_W-8yGDqxkhoia6Joy-QBuqFa8aLflLtCmcrqgU8gq9SWlPCGlaQV-jKyoZ44K3G_Tn1gf3CJN3dsSHGA4Qs4eEw4C3Sj9sW_mA4-PublexL_gG92HpRsCH4OdcTUu2Gfr_79jPLoJN53R39GFJ4wn7nLB12R99Pr1FrwY7Jni3ntfo9-7br-336v7n3Y_tzX3lGtbkSjBLNRdOdrRcLeXMOZBAFHWtZr2iSjaOcEmYFFxzJaxQWhALmvEBqOTX6NOlbpnn7wIpm8knB-NoZyhdGamkaLgWz4K0VaohkhVQXEAXQ0oRBnOIfrLxZCgxZx1mb1Yd5qzDEG2KjpL7sH6wdBP0T6l1_wX4uAI2FQNDtLPz6YlTQkhFz4W-Xjgoezt6iCY5D7OD3kdw2fTBP9PKP0iWqH8</recordid><startdate>20060224</startdate><enddate>20060224</enddate><creator>Wang, Ju</creator><creator>Hong, An</creator><creator>Ren, Jin-song</creator><creator>Sun, Fen-Yong</creator><creator>Shi, Ying-jiao</creator><creator>Liu, Kan</creator><creator>Xie, Qiu-Ling</creator><creator>Dai, Yun</creator><creator>Li, Zhi-ying</creator><creator>Chen, Yu</creator><general>Elsevier B.V</general><general>Elsevier</general><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>7QL</scope><scope>7QO</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20060224</creationdate><title>Biochemical properties of C78SC96S rhFGF-2: A double point-mutated rhFGF-2 increases obviously its activity</title><author>Wang, Ju ; Hong, An ; Ren, Jin-song ; Sun, Fen-Yong ; Shi, Ying-jiao ; Liu, Kan ; Xie, Qiu-Ling ; Dai, Yun ; Li, Zhi-ying ; Chen, Yu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c424t-52a1835c6b152aa132cce6e071c982d71764c036026538375a57850ae823fe163</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>3T3 Cells</topic><topic>Amino Acid Substitution</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Cell Proliferation - drug effects</topic><topic>Escherichia coli</topic><topic>Fibroblast Growth Factor 2 - chemistry</topic><topic>Fibroblast Growth Factor 2 - genetics</topic><topic>Fibroblast Growth Factor 2 - pharmacology</topic><topic>Fluorescence spectroscopy</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Mice</topic><topic>Mitogenic activity</topic><topic>Mutation</topic><topic>Point Mutation</topic><topic>Protein Structure, Secondary - genetics</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - pharmacology</topic><topic>rhFGF-2</topic><topic>Structure-Activity Relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, Ju</creatorcontrib><creatorcontrib>Hong, An</creatorcontrib><creatorcontrib>Ren, Jin-song</creatorcontrib><creatorcontrib>Sun, Fen-Yong</creatorcontrib><creatorcontrib>Shi, Ying-jiao</creatorcontrib><creatorcontrib>Liu, Kan</creatorcontrib><creatorcontrib>Xie, Qiu-Ling</creatorcontrib><creatorcontrib>Dai, Yun</creatorcontrib><creatorcontrib>Li, Zhi-ying</creatorcontrib><creatorcontrib>Chen, Yu</creatorcontrib><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>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, Ju</au><au>Hong, An</au><au>Ren, Jin-song</au><au>Sun, Fen-Yong</au><au>Shi, Ying-jiao</au><au>Liu, Kan</au><au>Xie, Qiu-Ling</au><au>Dai, Yun</au><au>Li, Zhi-ying</au><au>Chen, Yu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Biochemical properties of C78SC96S rhFGF-2: A double point-mutated rhFGF-2 increases obviously its activity</atitle><jtitle>Journal of biotechnology</jtitle><addtitle>J Biotechnol</addtitle><date>2006-02-24</date><risdate>2006</risdate><volume>121</volume><issue>4</issue><spage>442</spage><epage>447</epage><pages>442-447</pages><issn>0168-1656</issn><eissn>1873-4863</eissn><coden>JBITD4</coden><abstract>Fibroblast growth factor-2 (FGF-2) is a multifunctional polypeptide that affects many cellular functions and phenomena. The wild-type recombinant human fibroblast growth factor rhFGF-2
W and the mutant C78SC96S rhFGF-2
M were expressed in
Escherichia coli and their products were purified. The results by the means of fluorescence spectroscopy and CD spectrums, suggested that due to its decreased hydrophobicity rhFGF-2 is not deposited as an inclusion body. The mitogenic activity of the expressed rhFGF-2
M on 3T3 fibroblasts was shown to be 10-fold more than the expressed rhFGF-2
W of which the biological activity was a little less than that of the standard rhbFGF
W, indicating that the increased biological activity was due to the change of its secondary structure, dimerization and affinity binding to FGF receptor (FGFR).</abstract><cop>Lausanne</cop><cop>Amsterdam</cop><cop>New York, NY</cop><pub>Elsevier B.V</pub><pmid>16223539</pmid><doi>10.1016/j.jbiotec.2005.08.021</doi><tpages>6</tpages></addata></record> |
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| identifier | ISSN: 0168-1656 |
| ispartof | Journal of biotechnology, 2006-02, Vol.121 (4), p.442-447 |
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| subjects | 3T3 Cells Amino Acid Substitution Animals Biological and medical sciences Biotechnology Cell Proliferation - drug effects Escherichia coli Fibroblast Growth Factor 2 - chemistry Fibroblast Growth Factor 2 - genetics Fibroblast Growth Factor 2 - pharmacology Fluorescence spectroscopy Fundamental and applied biological sciences. Psychology Humans Mice Mitogenic activity Mutation Point Mutation Protein Structure, Secondary - genetics Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - pharmacology rhFGF-2 Structure-Activity Relationship |
| title | Biochemical properties of C78SC96S rhFGF-2: A double point-mutated rhFGF-2 increases obviously its activity |
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