Cloning and expression of the cDNA coding for aequorin, a bioluminescent calcium-binding protein
Aequorin is a bioluminescent protein which consists of a polypeptide chain (apoaequorin), coelenterate luciferin, and bound oxygen. Aequorin produces blue light upon binding Ca 2+. We have isolated six recombinant pBR322 plasmids which contain apoaequorin cDNA sequences. A mixed synthetic oligonucle...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1985-02, Vol.126 (3), p.1259-1268 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Prasher, Douglas McCann, Richard O. Cormier, Milton J. |
| description | Aequorin is a bioluminescent protein which consists of a polypeptide chain (apoaequorin), coelenterate luciferin, and bound oxygen. Aequorin produces blue light upon binding Ca
2+. We have isolated six recombinant pBR322 plasmids which contain apoaequorin cDNA sequences. A mixed synthetic oligonucleotide probe was used to identify these cDNAs. An extract of an
E
.
coli
strain possessing the largest cDNA contained apoaequorin. This apoaequorin can be converted to aequorin in the presence of coelenterate luciferin, 2-mercaptoethanol, and O
2. This cDNA is therefore apparently full-length. |
| doi_str_mv | 10.1016/0006-291X(85)90321-3 |
| format | Article |
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2+. We have isolated six recombinant pBR322 plasmids which contain apoaequorin cDNA sequences. A mixed synthetic oligonucleotide probe was used to identify these cDNAs. An extract of an
E
.
coli
strain possessing the largest cDNA contained apoaequorin. This apoaequorin can be converted to aequorin in the presence of coelenterate luciferin, 2-mercaptoethanol, and O
2. This cDNA is therefore apparently full-length.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(85)90321-3</identifier><identifier>PMID: 2579647</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Aequorea victoria ; Aequorin - genetics ; Base Sequence ; Cloning, Molecular ; DNA ; Escherichia coli - genetics ; Gene Expression Regulation ; Luminescent Proteins - genetics ; Peptides - isolation & purification ; Poly A - metabolism ; Protein Biosynthesis ; RNA - metabolism ; RNA, Messenger</subject><ispartof>Biochemical and biophysical research communications, 1985-02, Vol.126 (3), p.1259-1268</ispartof><rights>1985</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c454t-224c2d1c0d09e1efa03bddc31cda39c1ae3ae467321754c7b3a81953e35e10e93</citedby><cites>FETCH-LOGICAL-c454t-224c2d1c0d09e1efa03bddc31cda39c1ae3ae467321754c7b3a81953e35e10e93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0006-291X(85)90321-3$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2579647$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Prasher, Douglas</creatorcontrib><creatorcontrib>McCann, Richard O.</creatorcontrib><creatorcontrib>Cormier, Milton J.</creatorcontrib><title>Cloning and expression of the cDNA coding for aequorin, a bioluminescent calcium-binding protein</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Aequorin is a bioluminescent protein which consists of a polypeptide chain (apoaequorin), coelenterate luciferin, and bound oxygen. Aequorin produces blue light upon binding Ca
2+. We have isolated six recombinant pBR322 plasmids which contain apoaequorin cDNA sequences. A mixed synthetic oligonucleotide probe was used to identify these cDNAs. An extract of an
E
.
coli
strain possessing the largest cDNA contained apoaequorin. This apoaequorin can be converted to aequorin in the presence of coelenterate luciferin, 2-mercaptoethanol, and O
2. This cDNA is therefore apparently full-length.</description><subject>Aequorea victoria</subject><subject>Aequorin - genetics</subject><subject>Base Sequence</subject><subject>Cloning, Molecular</subject><subject>DNA</subject><subject>Escherichia coli - genetics</subject><subject>Gene Expression Regulation</subject><subject>Luminescent Proteins - genetics</subject><subject>Peptides - isolation & purification</subject><subject>Poly A - metabolism</subject><subject>Protein Biosynthesis</subject><subject>RNA - metabolism</subject><subject>RNA, Messenger</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1985</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUFP3DAQhS1URLeUf0AlnyoqkXYmdpL1BQltS6mE4FIkbsaxJ62rxF7sBMG_b5ZdcWxPc5jvvZl5w9gxwmcErL8AQF2UCu9OltUnBaLEQuyxBYKCokSQb9jiFXnL3uX8BwBR1uqAHZRVo2rZLNj9qo_Bh1_cBMfpaZ0oZx8Djx0ffxO3X6_PuY1uQ3QxcUMPU0w-nHLDWx_7afCBsqUwcmt666ehaH14wdcpjuTDe7bfmT7T0a4estuLbz9Xl8XVzfcfq_OrwspKjkVZSls6tOBAEVJnQLTOWYHWGaEsGhKGZN3MVzaVtE0rzBJVJUhUhEBKHLKPW9957sNEedSDnxfrexMoTlk3NZSing3-B6JErATCDMotaFPMOVGn18kPJj1rBL35gN7Eqzfx6mWlXz6gxSz7sPOf2oHcq2gX-dw_2_ZpTuPRU9LZegqWnE9kR-2i__eAv6GBlZw</recordid><startdate>19850215</startdate><enddate>19850215</enddate><creator>Prasher, Douglas</creator><creator>McCann, Richard O.</creator><creator>Cormier, Milton J.</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>7TM</scope><scope>7X8</scope></search><sort><creationdate>19850215</creationdate><title>Cloning and expression of the cDNA coding for aequorin, a bioluminescent calcium-binding protein</title><author>Prasher, Douglas ; McCann, Richard O. ; Cormier, Milton J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c454t-224c2d1c0d09e1efa03bddc31cda39c1ae3ae467321754c7b3a81953e35e10e93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1985</creationdate><topic>Aequorea victoria</topic><topic>Aequorin - genetics</topic><topic>Base Sequence</topic><topic>Cloning, Molecular</topic><topic>DNA</topic><topic>Escherichia coli - genetics</topic><topic>Gene Expression Regulation</topic><topic>Luminescent Proteins - genetics</topic><topic>Peptides - isolation & purification</topic><topic>Poly A - metabolism</topic><topic>Protein Biosynthesis</topic><topic>RNA - metabolism</topic><topic>RNA, Messenger</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Prasher, Douglas</creatorcontrib><creatorcontrib>McCann, Richard O.</creatorcontrib><creatorcontrib>Cormier, Milton J.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</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>Prasher, Douglas</au><au>McCann, Richard O.</au><au>Cormier, Milton J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning and expression of the cDNA coding for aequorin, a bioluminescent calcium-binding protein</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1985-02-15</date><risdate>1985</risdate><volume>126</volume><issue>3</issue><spage>1259</spage><epage>1268</epage><pages>1259-1268</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Aequorin is a bioluminescent protein which consists of a polypeptide chain (apoaequorin), coelenterate luciferin, and bound oxygen. Aequorin produces blue light upon binding Ca
2+. We have isolated six recombinant pBR322 plasmids which contain apoaequorin cDNA sequences. A mixed synthetic oligonucleotide probe was used to identify these cDNAs. An extract of an
E
.
coli
strain possessing the largest cDNA contained apoaequorin. This apoaequorin can be converted to aequorin in the presence of coelenterate luciferin, 2-mercaptoethanol, and O
2. This cDNA is therefore apparently full-length.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>2579647</pmid><doi>10.1016/0006-291X(85)90321-3</doi><tpages>10</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 1985-02, Vol.126 (3), p.1259-1268 |
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| language | eng |
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| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Aequorea victoria Aequorin - genetics Base Sequence Cloning, Molecular DNA Escherichia coli - genetics Gene Expression Regulation Luminescent Proteins - genetics Peptides - isolation & purification Poly A - metabolism Protein Biosynthesis RNA - metabolism RNA, Messenger |
| title | Cloning and expression of the cDNA coding for aequorin, a bioluminescent calcium-binding protein |
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