The use of 4-(2-pyridylazo)resorcinol in studies of zinc release from Escherichia coli aspartate transcarbamoylase
The metallochromic indicator 4-(2-pyridylazo)resorcinol (PAR) has been used at pH 7.0 to monitor the mercurial-promoted Zn 2+ release from Escherichia coli aspartate transcarbamoylase and Zn 2+ uptake by regulatory dimers upon displacement of the mercurial reagent with 2-mercaptoethanol. The release...
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| Veröffentlicht in: | Analytical biochemistry 1985-04, Vol.146 (1), p.150-157 |
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| container_title | Analytical biochemistry |
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| creator | Hunt, John B. Neece, Sue H. Ginsburg, Ann |
| description | The metallochromic indicator 4-(2-pyridylazo)resorcinol (PAR) has been used at pH 7.0 to monitor the mercurial-promoted Zn
2+ release from
Escherichia coli aspartate transcarbamoylase and Zn
2+ uptake by regulatory dimers upon displacement of the mercurial reagent with 2-mercaptoethanol. The release of Zn
2+ (as reflected by a yellow to orange color change in PAR solutions) is linked to dissociation of the enzyme since the six Zn
2+ bonding domains stabilize catalytic and regulatory chain contacts; the rebinding of Zn
2+ produces enzyme assembly and a corresponding decrease in the amount of PAR-Zn
2+ complex. Using 10-fold PAR to free Zn
2+ at pH 7.0, Δϵ = 6.6 ± 0.2 × 10
4
m
−1 cm
−1 at 500 nm (20°C) for (PAR)
2Zn
2+ complex formation (β
2
′ ≅ 10
12
m
−1). In kinetic studies at pH 7.0, PAR (10
−4
m) has been used to measure the instantaneous concentration of Zn
2+ released from micromolar quantities of protein; second-order
k = 2 × 10
7
m
−1 s
−1 for forming the 1:1 PAR:Zn
2+ complex. These properties of PAR-Zn
2+ interactions make PAR a generally useful reagent for studying Zn
2+ release from proteins. |
| doi_str_mv | 10.1016/0003-2697(85)90409-9 |
| format | Article |
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2+ release from
Escherichia coli aspartate transcarbamoylase and Zn
2+ uptake by regulatory dimers upon displacement of the mercurial reagent with 2-mercaptoethanol. The release of Zn
2+ (as reflected by a yellow to orange color change in PAR solutions) is linked to dissociation of the enzyme since the six Zn
2+ bonding domains stabilize catalytic and regulatory chain contacts; the rebinding of Zn
2+ produces enzyme assembly and a corresponding decrease in the amount of PAR-Zn
2+ complex. Using 10-fold PAR to free Zn
2+ at pH 7.0, Δϵ = 6.6 ± 0.2 × 10
4
m
−1 cm
−1 at 500 nm (20°C) for (PAR)
2Zn
2+ complex formation (β
2
′ ≅ 10
12
m
−1). In kinetic studies at pH 7.0, PAR (10
−4
m) has been used to measure the instantaneous concentration of Zn
2+ released from micromolar quantities of protein; second-order
k = 2 × 10
7
m
−1 s
−1 for forming the 1:1 PAR:Zn
2+ complex. These properties of PAR-Zn
2+ interactions make PAR a generally useful reagent for studying Zn
2+ release from proteins.</description><identifier>ISSN: 0003-2697</identifier><identifier>EISSN: 1096-0309</identifier><identifier>DOI: 10.1016/0003-2697(85)90409-9</identifier><identifier>PMID: 3887984</identifier><identifier>CODEN: ANBCA2</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>4-(2-pyridylazo)resorcinol ; Applied sciences ; Aspartate Carbamoyltransferase - metabolism ; aspartate transcarbamoylase ; Chemical Phenomena ; Chemistry ; Escherichia coli ; Escherichia coli - enzymology ; Exact sciences and technology ; Other techniques and industries ; Resorcinols ; Spectrophotometry ; Spectrophotometry, Ultraviolet ; Zinc - analysis ; Zn 2</subject><ispartof>Analytical biochemistry, 1985-04, Vol.146 (1), p.150-157</ispartof><rights>1985</rights><rights>1986 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c483t-4974cadd8bbc92686caa72af79f3a35c632bcbd5832b2aa5d4dbd2e77d3bf9b53</citedby><cites>FETCH-LOGICAL-c483t-4974cadd8bbc92686caa72af79f3a35c632bcbd5832b2aa5d4dbd2e77d3bf9b53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0003269785904099$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8837852$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3887984$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hunt, John B.</creatorcontrib><creatorcontrib>Neece, Sue H.</creatorcontrib><creatorcontrib>Ginsburg, Ann</creatorcontrib><title>The use of 4-(2-pyridylazo)resorcinol in studies of zinc release from Escherichia coli aspartate transcarbamoylase</title><title>Analytical biochemistry</title><addtitle>Anal Biochem</addtitle><description>The metallochromic indicator 4-(2-pyridylazo)resorcinol (PAR) has been used at pH 7.0 to monitor the mercurial-promoted Zn
2+ release from
Escherichia coli aspartate transcarbamoylase and Zn
2+ uptake by regulatory dimers upon displacement of the mercurial reagent with 2-mercaptoethanol. The release of Zn
2+ (as reflected by a yellow to orange color change in PAR solutions) is linked to dissociation of the enzyme since the six Zn
2+ bonding domains stabilize catalytic and regulatory chain contacts; the rebinding of Zn
2+ produces enzyme assembly and a corresponding decrease in the amount of PAR-Zn
2+ complex. Using 10-fold PAR to free Zn
2+ at pH 7.0, Δϵ = 6.6 ± 0.2 × 10
4
m
−1 cm
−1 at 500 nm (20°C) for (PAR)
2Zn
2+ complex formation (β
2
′ ≅ 10
12
m
−1). In kinetic studies at pH 7.0, PAR (10
−4
m) has been used to measure the instantaneous concentration of Zn
2+ released from micromolar quantities of protein; second-order
k = 2 × 10
7
m
−1 s
−1 for forming the 1:1 PAR:Zn
2+ complex. These properties of PAR-Zn
2+ interactions make PAR a generally useful reagent for studying Zn
2+ release from proteins.</description><subject>4-(2-pyridylazo)resorcinol</subject><subject>Applied sciences</subject><subject>Aspartate Carbamoyltransferase - metabolism</subject><subject>aspartate transcarbamoylase</subject><subject>Chemical Phenomena</subject><subject>Chemistry</subject><subject>Escherichia coli</subject><subject>Escherichia coli - enzymology</subject><subject>Exact sciences and technology</subject><subject>Other techniques and industries</subject><subject>Resorcinols</subject><subject>Spectrophotometry</subject><subject>Spectrophotometry, Ultraviolet</subject><subject>Zinc - analysis</subject><subject>Zn 2</subject><issn>0003-2697</issn><issn>1096-0309</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1985</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtrFEEUhRtR4hj9Bwq1EEkWrfXqemwECYkKATdxXdyuus2UdHeNVd3C5Ndb4wyzNKu7ON85XM5pmreMfmSUqU-UUtFyZfWV6a4tldS29lmzYdSqlgpqnzebM_KyeVXKL0oZk526aC6EMdoauWnywxbJWpCkgcj2ire7fY5hP8Jjus5YUvZxTiOJMynLGiKWA_gYZ08yjgjVOOQ0kdvit5ij30YgPo2RQNlBXmBBsmSYi4fcw5RqbsHXzYsBxoJvTvey-Xl3-3Dzrb3_8fX7zZf71ksjllZaLT2EYPreW66M8gCaw6DtIEB0Xgne-z50pl4O0AUZ-sBR6yD6wfaduGw-HHN3Of1esSxuisXjOMKMaS1OK8Yo1-ZJkEmlNFeygvII-pxKyTi4XY4T5L1j1B02cYfC3aFwZzr3bxNnq-3dKX_tJwxn02mEqr8_6VCLGodamI_ljBkjtOl4xT4fMayl_YmYXfERZ48hZvSLCyn-_4-_Q56p9A</recordid><startdate>198504</startdate><enddate>198504</enddate><creator>Hunt, John B.</creator><creator>Neece, Sue H.</creator><creator>Ginsburg, Ann</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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>198504</creationdate><title>The use of 4-(2-pyridylazo)resorcinol in studies of zinc release from Escherichia coli aspartate transcarbamoylase</title><author>Hunt, John B. ; Neece, Sue H. ; Ginsburg, Ann</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c483t-4974cadd8bbc92686caa72af79f3a35c632bcbd5832b2aa5d4dbd2e77d3bf9b53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1985</creationdate><topic>4-(2-pyridylazo)resorcinol</topic><topic>Applied sciences</topic><topic>Aspartate Carbamoyltransferase - metabolism</topic><topic>aspartate transcarbamoylase</topic><topic>Chemical Phenomena</topic><topic>Chemistry</topic><topic>Escherichia coli</topic><topic>Escherichia coli - enzymology</topic><topic>Exact sciences and technology</topic><topic>Other techniques and industries</topic><topic>Resorcinols</topic><topic>Spectrophotometry</topic><topic>Spectrophotometry, Ultraviolet</topic><topic>Zinc - analysis</topic><topic>Zn 2</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hunt, John B.</creatorcontrib><creatorcontrib>Neece, Sue H.</creatorcontrib><creatorcontrib>Ginsburg, Ann</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>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Analytical biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hunt, John B.</au><au>Neece, Sue H.</au><au>Ginsburg, Ann</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The use of 4-(2-pyridylazo)resorcinol in studies of zinc release from Escherichia coli aspartate transcarbamoylase</atitle><jtitle>Analytical biochemistry</jtitle><addtitle>Anal Biochem</addtitle><date>1985-04</date><risdate>1985</risdate><volume>146</volume><issue>1</issue><spage>150</spage><epage>157</epage><pages>150-157</pages><issn>0003-2697</issn><eissn>1096-0309</eissn><coden>ANBCA2</coden><abstract>The metallochromic indicator 4-(2-pyridylazo)resorcinol (PAR) has been used at pH 7.0 to monitor the mercurial-promoted Zn
2+ release from
Escherichia coli aspartate transcarbamoylase and Zn
2+ uptake by regulatory dimers upon displacement of the mercurial reagent with 2-mercaptoethanol. The release of Zn
2+ (as reflected by a yellow to orange color change in PAR solutions) is linked to dissociation of the enzyme since the six Zn
2+ bonding domains stabilize catalytic and regulatory chain contacts; the rebinding of Zn
2+ produces enzyme assembly and a corresponding decrease in the amount of PAR-Zn
2+ complex. Using 10-fold PAR to free Zn
2+ at pH 7.0, Δϵ = 6.6 ± 0.2 × 10
4
m
−1 cm
−1 at 500 nm (20°C) for (PAR)
2Zn
2+ complex formation (β
2
′ ≅ 10
12
m
−1). In kinetic studies at pH 7.0, PAR (10
−4
m) has been used to measure the instantaneous concentration of Zn
2+ released from micromolar quantities of protein; second-order
k = 2 × 10
7
m
−1 s
−1 for forming the 1:1 PAR:Zn
2+ complex. These properties of PAR-Zn
2+ interactions make PAR a generally useful reagent for studying Zn
2+ release from proteins.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>3887984</pmid><doi>10.1016/0003-2697(85)90409-9</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0003-2697 |
| ispartof | Analytical biochemistry, 1985-04, Vol.146 (1), p.150-157 |
| issn | 0003-2697 1096-0309 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76110278 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | 4-(2-pyridylazo)resorcinol Applied sciences Aspartate Carbamoyltransferase - metabolism aspartate transcarbamoylase Chemical Phenomena Chemistry Escherichia coli Escherichia coli - enzymology Exact sciences and technology Other techniques and industries Resorcinols Spectrophotometry Spectrophotometry, Ultraviolet Zinc - analysis Zn 2 |
| title | The use of 4-(2-pyridylazo)resorcinol in studies of zinc release from Escherichia coli aspartate transcarbamoylase |
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