The binding of aminoacyl-tRNA synthetases to triazine dye conjugates
The binding of thirteen aminoacyl-tRNA synthetases to thirty two immobilised procion dyes has been investigated. Most dyes bind one or more enzymes. The amino acid substrates are not normally potent eluants, with the notable exception of tryptophan eluting tryptophanyl-tRNA synthetase from Brown MX-...
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Veröffentlicht in: | Nucleic acids research 1979-11, Vol.7 (6), p.1579-1591 |
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description | The binding of thirteen aminoacyl-tRNA synthetases to thirty two immobilised procion dyes has been investigated. Most dyes bind one or more enzymes. The amino acid substrates are not normally potent eluants, with the notable exception of tryptophan eluting tryptophanyl-tRNA synthetase from Brown MX-5BR. Phosphate is frequently extremely effective, much more than expected by simple considerations of ionic strength, indicating that many of the dyes are able to mimic the phosphate groups of the phosphodiester backbone of the nucleic acid. Procedures for the purification of methionyl-, tryptophanyl- and tyrosyl-tRNA synthetases are presented and compared to the conventional purifications of these enzymes. The results indicate the general applicability of these dye columns to the purification of most enzymes of nucleic acid metabolism and the necessity of investigating as many different dyes as possible for any individual enzyme. |
doi_str_mv | 10.1093/nar/7.6.1579 |
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Most dyes bind one or more enzymes. The amino acid substrates are not normally potent eluants, with the notable exception of tryptophan eluting tryptophanyl-tRNA synthetase from Brown MX-5BR. Phosphate is frequently extremely effective, much more than expected by simple considerations of ionic strength, indicating that many of the dyes are able to mimic the phosphate groups of the phosphodiester backbone of the nucleic acid. Procedures for the purification of methionyl-, tryptophanyl- and tyrosyl-tRNA synthetases are presented and compared to the conventional purifications of these enzymes. The results indicate the general applicability of these dye columns to the purification of most enzymes of nucleic acid metabolism and the necessity of investigating as many different dyes as possible for any individual enzyme.</description><identifier>ISSN: 0305-1048</identifier><identifier>EISSN: 1362-4962</identifier><identifier>DOI: 10.1093/nar/7.6.1579</identifier><identifier>PMID: 503862</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Amino Acyl-tRNA Synthetases - isolation & purification ; Amino Acyl-tRNA Synthetases - metabolism ; Binding Sites ; Coloring Agents - pharmacology ; Geobacillus stearothermophilus ; Protein Binding ; Structure-Activity Relationship ; Triazines - pharmacology</subject><ispartof>Nucleic acids research, 1979-11, Vol.7 (6), p.1579-1591</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3619-c0d7227a0a7ee5f990bc478a38366e8b7ba7761e701421f434f1af4024246a5f3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC342329/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC342329/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27903,27904,53769,53771</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/503862$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bruton, Chris J.</creatorcontrib><creatorcontrib>Atkinson, Tony</creatorcontrib><title>The binding of aminoacyl-tRNA synthetases to triazine dye conjugates</title><title>Nucleic acids research</title><addtitle>Nucleic Acids Res</addtitle><description>The binding of thirteen aminoacyl-tRNA synthetases to thirty two immobilised procion dyes has been investigated. Most dyes bind one or more enzymes. The amino acid substrates are not normally potent eluants, with the notable exception of tryptophan eluting tryptophanyl-tRNA synthetase from Brown MX-5BR. Phosphate is frequently extremely effective, much more than expected by simple considerations of ionic strength, indicating that many of the dyes are able to mimic the phosphate groups of the phosphodiester backbone of the nucleic acid. Procedures for the purification of methionyl-, tryptophanyl- and tyrosyl-tRNA synthetases are presented and compared to the conventional purifications of these enzymes. The results indicate the general applicability of these dye columns to the purification of most enzymes of nucleic acid metabolism and the necessity of investigating as many different dyes as possible for any individual enzyme.</description><subject>Amino Acyl-tRNA Synthetases - isolation & purification</subject><subject>Amino Acyl-tRNA Synthetases - metabolism</subject><subject>Binding Sites</subject><subject>Coloring Agents - pharmacology</subject><subject>Geobacillus stearothermophilus</subject><subject>Protein Binding</subject><subject>Structure-Activity Relationship</subject><subject>Triazines - pharmacology</subject><issn>0305-1048</issn><issn>1362-4962</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1979</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkb1PG0EQxVcRJBiSLmWKq1JxZr9u966gQA6JkSwQyEQozWruPGcvnHdhdx3h_PWcZWSFimqK93szb_QI-crokNFKnDgIJ3qohqzQ1QcyYELxXFaK75EBFbTIGZXlATmM8Z5SJlkhP5GPBRWl4gPyY7rArLZuZt08820GS-s8NOsuTzeXZ1lcu7TABBFjlnyWgoV_1mE2W2PWeHe_mkPC-Jnst9BF_PI6j8jtz_PpaJxPrn5djM4meSMUq_KGzjTnGihoxKKtKlo3UpcgSqEUlrWuQWvFUPcpOWulkC2DVlIuuVRQtOKInG73Pq7qJc4adClAZx6DXUJYGw_WvFWcXZi5_2uE5IJXvf_7qz_4pxXGZJY2Nth14NCvotFyc5-xd0FWCaVLqnrweAs2wccYsN2FYdRsyjF9OUYbZTbl9Pi3_x_Ywds2ejnfyjYmfN6pEB6M0kIXZnz3x6gRLcvp7ztzLV4AiByaDQ</recordid><startdate>19791124</startdate><enddate>19791124</enddate><creator>Bruton, Chris J.</creator><creator>Atkinson, Tony</creator><general>Oxford University Press</general><scope>BSCLL</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>7TM</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19791124</creationdate><title>The binding of aminoacyl-tRNA synthetases to triazine dye conjugates</title><author>Bruton, Chris J. ; Atkinson, Tony</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3619-c0d7227a0a7ee5f990bc478a38366e8b7ba7761e701421f434f1af4024246a5f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1979</creationdate><topic>Amino Acyl-tRNA Synthetases - isolation & purification</topic><topic>Amino Acyl-tRNA Synthetases - metabolism</topic><topic>Binding Sites</topic><topic>Coloring Agents - pharmacology</topic><topic>Geobacillus stearothermophilus</topic><topic>Protein Binding</topic><topic>Structure-Activity Relationship</topic><topic>Triazines - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bruton, Chris J.</creatorcontrib><creatorcontrib>Atkinson, Tony</creatorcontrib><collection>Istex</collection><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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Nucleic acids research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bruton, Chris J.</au><au>Atkinson, Tony</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The binding of aminoacyl-tRNA synthetases to triazine dye conjugates</atitle><jtitle>Nucleic acids research</jtitle><addtitle>Nucleic Acids Res</addtitle><date>1979-11-24</date><risdate>1979</risdate><volume>7</volume><issue>6</issue><spage>1579</spage><epage>1591</epage><pages>1579-1591</pages><issn>0305-1048</issn><eissn>1362-4962</eissn><abstract>The binding of thirteen aminoacyl-tRNA synthetases to thirty two immobilised procion dyes has been investigated. Most dyes bind one or more enzymes. The amino acid substrates are not normally potent eluants, with the notable exception of tryptophan eluting tryptophanyl-tRNA synthetase from Brown MX-5BR. Phosphate is frequently extremely effective, much more than expected by simple considerations of ionic strength, indicating that many of the dyes are able to mimic the phosphate groups of the phosphodiester backbone of the nucleic acid. Procedures for the purification of methionyl-, tryptophanyl- and tyrosyl-tRNA synthetases are presented and compared to the conventional purifications of these enzymes. The results indicate the general applicability of these dye columns to the purification of most enzymes of nucleic acid metabolism and the necessity of investigating as many different dyes as possible for any individual enzyme.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>503862</pmid><doi>10.1093/nar/7.6.1579</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acyl-tRNA Synthetases - isolation & purification Amino Acyl-tRNA Synthetases - metabolism Binding Sites Coloring Agents - pharmacology Geobacillus stearothermophilus Protein Binding Structure-Activity Relationship Triazines - pharmacology |
title | The binding of aminoacyl-tRNA synthetases to triazine dye conjugates |
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