Gene synthesis and expression in E. coli for pump, a human matrix metalloproteinase
The gene for PUMP ( putative metalloproteinase), a human matrix metalloproteinase, was synthesized by a PCR-based method. The DNA fragment of 546 bases containing the PUMP gene was generated by overlap extension of six long oligonucleotides (length ranging from 101 to 116 bases) and subsequent ampli...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1992-07, Vol.186 (1), p.143-149 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Ye, Qi-Zhuang Johnson, Linda L. Baragi, Vijaykumar |
| description | The gene for PUMP (
putative
metalloproteinase), a human matrix metalloproteinase, was synthesized by a PCR-based method. The DNA fragment of 546 bases containing the PUMP gene was generated by overlap extension of six long oligonucleotides (length ranging from 101 to 116 bases) and subsequent amplification by two short terminal oligonucleotide primers (length from 20 to 48 bases) in one pot without using restriction and ligation enzymes. The synthetic gene was cloned into a T7 expression vector in two ways to express PUMP as a non-fusion protein. Both constructs showed high level expression in
E. coli. |
| doi_str_mv | 10.1016/S0006-291X(05)80786-7 |
| format | Article |
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putative
metalloproteinase), a human matrix metalloproteinase, was synthesized by a PCR-based method. The DNA fragment of 546 bases containing the PUMP gene was generated by overlap extension of six long oligonucleotides (length ranging from 101 to 116 bases) and subsequent amplification by two short terminal oligonucleotide primers (length from 20 to 48 bases) in one pot without using restriction and ligation enzymes. The synthetic gene was cloned into a T7 expression vector in two ways to express PUMP as a non-fusion protein. Both constructs showed high level expression in
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putative
metalloproteinase), a human matrix metalloproteinase, was synthesized by a PCR-based method. The DNA fragment of 546 bases containing the PUMP gene was generated by overlap extension of six long oligonucleotides (length ranging from 101 to 116 bases) and subsequent amplification by two short terminal oligonucleotide primers (length from 20 to 48 bases) in one pot without using restriction and ligation enzymes. The synthetic gene was cloned into a T7 expression vector in two ways to express PUMP as a non-fusion protein. Both constructs showed high level expression in
E. coli.</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Cloning, Molecular - methods</subject><subject>DNA - genetics</subject><subject>DNA - isolation & purification</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Escherichia coli - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression</subject><subject>Genes, Synthetic</subject><subject>Humans</subject><subject>Hydrolases</subject><subject>Matrix Metalloproteinase 7</subject><subject>Metalloendopeptidases - genetics</subject><subject>Metalloendopeptidases - isolation & purification</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Oligodeoxyribonucleotides</subject><subject>Plasmids</subject><subject>Polymerase Chain Reaction - methods</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Restriction Mapping</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1r1UAUhgdR6vXqTyjMQkTB1DOZzCSzEim1CgUXVXA3nExO6EgyiXMSaf-9ae-lLl2dxfucr0eIUwVnCpT9cA0Atiid-vkWzLsG6sYW9ROxU-CgKBVUT8XuEXkuXjD_AlCqsu5EnCiry9rqnbi-pESS79JyQxxZYuok3c6ZmOOUZEzy4kyGaYiyn7Kc13F-L1HerCMmOeKS460cacFhmOY8LRQTMr0Uz3ocmF4d6178-Hzx_fxLcfXt8uv5p6si6BqWwqq2da7XwWJV6rqyGDT2oXUI2rrO9MbV1jUaXU8W665tui2gCkxDFZZG78Wbw9xt9e-VePFj5EDDgImmlX2twRptmg00BzDkiTlT7-ccR8x3XoG_l-kfZPp7Ux6Mf5C5te_F6XHB2o7U_es62Nvy18ccOeDQZ0wh8iNmKgvbpxv28YDRJuNPpOw5REqBupgpLL6b4n8O-QvdlJDj</recordid><startdate>19920715</startdate><enddate>19920715</enddate><creator>Ye, Qi-Zhuang</creator><creator>Johnson, Linda L.</creator><creator>Baragi, Vijaykumar</creator><general>Elsevier Inc</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>7X8</scope></search><sort><creationdate>19920715</creationdate><title>Gene synthesis and expression in E. coli for pump, a human matrix metalloproteinase</title><author>Ye, Qi-Zhuang ; Johnson, Linda L. ; Baragi, Vijaykumar</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c370t-61bb99f3c6a423746ac3afcb9a0369d5f5976983a9fe6a7db8d036e4058e4a253</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Cloning, Molecular - methods</topic><topic>DNA - genetics</topic><topic>DNA - isolation & purification</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Escherichia coli - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression</topic><topic>Genes, Synthetic</topic><topic>Humans</topic><topic>Hydrolases</topic><topic>Matrix Metalloproteinase 7</topic><topic>Metalloendopeptidases - genetics</topic><topic>Metalloendopeptidases - isolation & purification</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Oligodeoxyribonucleotides</topic><topic>Plasmids</topic><topic>Polymerase Chain Reaction - methods</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Restriction Mapping</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ye, Qi-Zhuang</creatorcontrib><creatorcontrib>Johnson, Linda L.</creatorcontrib><creatorcontrib>Baragi, Vijaykumar</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>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ye, Qi-Zhuang</au><au>Johnson, Linda L.</au><au>Baragi, Vijaykumar</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Gene synthesis and expression in E. coli for pump, a human matrix metalloproteinase</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1992-07-15</date><risdate>1992</risdate><volume>186</volume><issue>1</issue><spage>143</spage><epage>149</epage><pages>143-149</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><coden>BBRCA9</coden><abstract>The gene for PUMP (
putative
metalloproteinase), a human matrix metalloproteinase, was synthesized by a PCR-based method. The DNA fragment of 546 bases containing the PUMP gene was generated by overlap extension of six long oligonucleotides (length ranging from 101 to 116 bases) and subsequent amplification by two short terminal oligonucleotide primers (length from 20 to 48 bases) in one pot without using restriction and ligation enzymes. The synthetic gene was cloned into a T7 expression vector in two ways to express PUMP as a non-fusion protein. Both constructs showed high level expression in
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| ispartof | Biochemical and biophysical research communications, 1992-07, Vol.186 (1), p.143-149 |
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| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry Biological and medical sciences Cloning, Molecular - methods DNA - genetics DNA - isolation & purification Enzymes and enzyme inhibitors Escherichia coli - genetics Fundamental and applied biological sciences. Psychology Gene Expression Genes, Synthetic Humans Hydrolases Matrix Metalloproteinase 7 Metalloendopeptidases - genetics Metalloendopeptidases - isolation & purification Molecular Sequence Data Molecular Weight Oligodeoxyribonucleotides Plasmids Polymerase Chain Reaction - methods Recombinant Proteins - isolation & purification Restriction Mapping |
| title | Gene synthesis and expression in E. coli for pump, a human matrix metalloproteinase |
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