Lactose repressor protein reaction with 2-chloromercuri-4-nitrophenol
Reaction of the lactose repressor protein with 2-chloromercuri-4-nitrophenol resulted in modification of two of the three cysteine residues per monomer at all pH values tested. At pH 8.1 it was possible to detect two equivalence points, corresponding to one and two mercurinitrophenol residues introd...
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| Veröffentlicht in: | Journal of molecular biology 1976-05, Vol.103 (2), p.433-437 |
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| container_end_page | 437 |
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| container_title | Journal of molecular biology |
| container_volume | 103 |
| creator | Yang, Diana S. Matthews, Kathleen S. |
| description | Reaction of the lactose repressor protein with 2-chloromercuri-4-nitrophenol resulted in modification of two of the three cysteine residues per monomer at all pH values tested. At pH 8.1 it was possible to detect two equivalence points, corresponding to one and two mercurinitrophenol residues introduced per monomer. Inducer and operator binding activities were not affected by the introduction of the mercurial into the protein structure. Inducer binding, but not anti-inducer binding, produced a change in the spectrum of the mercurinitrophenol, apparently due to alterations in the environment of the chromophores as a result of shifts in the structure of the repressor protein. |
| doi_str_mv | 10.1016/0022-2836(76)90322-3 |
| format | Article |
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At pH 8.1 it was possible to detect two equivalence points, corresponding to one and two mercurinitrophenol residues introduced per monomer. Inducer and operator binding activities were not affected by the introduction of the mercurial into the protein structure. Inducer binding, but not anti-inducer binding, produced a change in the spectrum of the mercurinitrophenol, apparently due to alterations in the environment of the chromophores as a result of shifts in the structure of the repressor protein.</description><identifier>ISSN: 0022-2836</identifier><identifier>EISSN: 1089-8638</identifier><identifier>DOI: 10.1016/0022-2836(76)90322-3</identifier><identifier>PMID: 781275</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Bacterial Proteins - metabolism ; Binding Sites ; Escherichia coli - metabolism ; Kinetics ; Lactose - metabolism ; Macromolecular Substances ; Mercury ; Nitrophenols ; Organometallic Compounds ; Protein Binding ; Protein Conformation ; Spectrophotometry ; Spectrophotometry, Ultraviolet</subject><ispartof>Journal of molecular biology, 1976-05, Vol.103 (2), p.433-437</ispartof><rights>1976</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c356t-24636dc2a2bd3f6403f5401d9b7526cb734ba63760c0b29a50b20024e96c4ee03</citedby><cites>FETCH-LOGICAL-c356t-24636dc2a2bd3f6403f5401d9b7526cb734ba63760c0b29a50b20024e96c4ee03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0022283676903223$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/781275$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yang, Diana S.</creatorcontrib><creatorcontrib>Matthews, Kathleen S.</creatorcontrib><title>Lactose repressor protein reaction with 2-chloromercuri-4-nitrophenol</title><title>Journal of molecular biology</title><addtitle>J Mol Biol</addtitle><description>Reaction of the lactose repressor protein with 2-chloromercuri-4-nitrophenol resulted in modification of two of the three cysteine residues per monomer at all pH values tested. At pH 8.1 it was possible to detect two equivalence points, corresponding to one and two mercurinitrophenol residues introduced per monomer. Inducer and operator binding activities were not affected by the introduction of the mercurial into the protein structure. Inducer binding, but not anti-inducer binding, produced a change in the spectrum of the mercurinitrophenol, apparently due to alterations in the environment of the chromophores as a result of shifts in the structure of the repressor protein.</description><subject>Bacterial Proteins - metabolism</subject><subject>Binding Sites</subject><subject>Escherichia coli - metabolism</subject><subject>Kinetics</subject><subject>Lactose - metabolism</subject><subject>Macromolecular Substances</subject><subject>Mercury</subject><subject>Nitrophenols</subject><subject>Organometallic Compounds</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Spectrophotometry</subject><subject>Spectrophotometry, Ultraviolet</subject><issn>0022-2836</issn><issn>1089-8638</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1976</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMtOwzAQRS3EqxT-oIusECwMfifZIFVVeUiV2MDaSpyJapTEwU5A_D0uqbpkM9b43rmaOQgtKLmjhKp7QhjDLOPqJlW3OeGx40doRkmW40zx7BjNDpZzdBHCByFEcpGdodM0oyyVM7TeFGZwARIPvYcQnE967wawXfyJknVd8m2HbcKw2TbOuxa8Gb3FAnd28K7fQueaS3RSF02Aq_07R--P67fVM968Pr2slhtsuFQDZkJxVRlWsLLitRKE11IQWuVlKpkyZcpFWSieKmJIyfJCxhovEJArIwAIn6PrKTfu-DlCGHRrg4GmKTpwY9AZF1IqSqNRTEbjXQgeat172xb-R1Oid_D0jozekdGp0n_wNI9ji33-WLZQHYYmWlF-mGSIN35Z8DoYC52Bynowg66c_T__F9zRfVo</recordid><startdate>19760515</startdate><enddate>19760515</enddate><creator>Yang, Diana S.</creator><creator>Matthews, Kathleen S.</creator><general>Elsevier Ltd</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>19760515</creationdate><title>Lactose repressor protein reaction with 2-chloromercuri-4-nitrophenol</title><author>Yang, Diana S. ; Matthews, Kathleen S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c356t-24636dc2a2bd3f6403f5401d9b7526cb734ba63760c0b29a50b20024e96c4ee03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1976</creationdate><topic>Bacterial Proteins - metabolism</topic><topic>Binding Sites</topic><topic>Escherichia coli - metabolism</topic><topic>Kinetics</topic><topic>Lactose - metabolism</topic><topic>Macromolecular Substances</topic><topic>Mercury</topic><topic>Nitrophenols</topic><topic>Organometallic Compounds</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Spectrophotometry</topic><topic>Spectrophotometry, Ultraviolet</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yang, Diana S.</creatorcontrib><creatorcontrib>Matthews, Kathleen S.</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>Journal of molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yang, Diana S.</au><au>Matthews, Kathleen S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Lactose repressor protein reaction with 2-chloromercuri-4-nitrophenol</atitle><jtitle>Journal of molecular biology</jtitle><addtitle>J Mol Biol</addtitle><date>1976-05-15</date><risdate>1976</risdate><volume>103</volume><issue>2</issue><spage>433</spage><epage>437</epage><pages>433-437</pages><issn>0022-2836</issn><eissn>1089-8638</eissn><abstract>Reaction of the lactose repressor protein with 2-chloromercuri-4-nitrophenol resulted in modification of two of the three cysteine residues per monomer at all pH values tested. At pH 8.1 it was possible to detect two equivalence points, corresponding to one and two mercurinitrophenol residues introduced per monomer. Inducer and operator binding activities were not affected by the introduction of the mercurial into the protein structure. Inducer binding, but not anti-inducer binding, produced a change in the spectrum of the mercurinitrophenol, apparently due to alterations in the environment of the chromophores as a result of shifts in the structure of the repressor protein.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>781275</pmid><doi>10.1016/0022-2836(76)90322-3</doi><tpages>5</tpages></addata></record> |
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| ispartof | Journal of molecular biology, 1976-05, Vol.103 (2), p.433-437 |
| issn | 0022-2836 1089-8638 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Bacterial Proteins - metabolism Binding Sites Escherichia coli - metabolism Kinetics Lactose - metabolism Macromolecular Substances Mercury Nitrophenols Organometallic Compounds Protein Binding Protein Conformation Spectrophotometry Spectrophotometry, Ultraviolet |
| title | Lactose repressor protein reaction with 2-chloromercuri-4-nitrophenol |
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