Parvalbumin conformers revealed by steady-state and time-resolved fluorescence spectroscopy
The binding of calcium to whiting (one tryptophan residue) and pike (one tyrosine residue) parvalbumins has been studied by means of kinetic and steady-state fluorescence techniques. The decay curves of the tryptophan and tyrosine fluorescence of the parvalbumins are best fitted by a sum of two expo...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 1985-08, Vol.240 (2), p.781-791 |
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| container_title | Archives of biochemistry and biophysics |
| container_volume | 240 |
| creator | Permyakov, E.A. Ostrovsky, A.V. Burstein, E.A. Pleshanov, P.G. Gerday, Ch |
| description | The binding of calcium to whiting (one tryptophan residue) and pike (one tyrosine residue) parvalbumins has been studied by means of kinetic and steady-state fluorescence techniques. The decay curves of the tryptophan and tyrosine fluorescence of the parvalbumins are best fitted by a sum of two exponents for any metal state of the proteins. The data can be interpreted as a nonexponential decay of the fluorescence of a single-type chromophore or in terms of equilibria between compact and relaxed conformers of the parvalbumins in each metal state. Fluorescence quenching by I
− ions and effects of H
20/D
20 substitution confirm the second interpretation. The constants of the equilibria have been evaluated. |
| doi_str_mv | 10.1016/0003-9861(85)90087-6 |
| format | Article |
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− ions and effects of H
20/D
20 substitution confirm the second interpretation. The constants of the equilibria have been evaluated.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/0003-9861(85)90087-6</identifier><identifier>PMID: 3927843</identifier><identifier>CODEN: ABBIA4</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>Animals ; Applied sciences ; Calcium - metabolism ; Egtazic Acid ; Exact sciences and technology ; Fishes - metabolism ; Iodine ; Isoelectric Point ; Kinetics ; Mathematics ; Muscle Proteins - metabolism ; Other techniques and industries ; Parvalbumins - metabolism ; Spectrometry, Fluorescence</subject><ispartof>Archives of biochemistry and biophysics, 1985-08, Vol.240 (2), p.781-791</ispartof><rights>1985</rights><rights>1986 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c386t-c6fda84bb45067e0938ff2474eba309ac895bd352fb736a9a331b01e3b09a01b3</citedby><cites>FETCH-LOGICAL-c386t-c6fda84bb45067e0938ff2474eba309ac895bd352fb736a9a331b01e3b09a01b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0003-9861(85)90087-6$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8840278$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3927843$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Permyakov, E.A.</creatorcontrib><creatorcontrib>Ostrovsky, A.V.</creatorcontrib><creatorcontrib>Burstein, E.A.</creatorcontrib><creatorcontrib>Pleshanov, P.G.</creatorcontrib><creatorcontrib>Gerday, Ch</creatorcontrib><title>Parvalbumin conformers revealed by steady-state and time-resolved fluorescence spectroscopy</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>The binding of calcium to whiting (one tryptophan residue) and pike (one tyrosine residue) parvalbumins has been studied by means of kinetic and steady-state fluorescence techniques. The decay curves of the tryptophan and tyrosine fluorescence of the parvalbumins are best fitted by a sum of two exponents for any metal state of the proteins. The data can be interpreted as a nonexponential decay of the fluorescence of a single-type chromophore or in terms of equilibria between compact and relaxed conformers of the parvalbumins in each metal state. Fluorescence quenching by I
− ions and effects of H
20/D
20 substitution confirm the second interpretation. The constants of the equilibria have been evaluated.</description><subject>Animals</subject><subject>Applied sciences</subject><subject>Calcium - metabolism</subject><subject>Egtazic Acid</subject><subject>Exact sciences and technology</subject><subject>Fishes - metabolism</subject><subject>Iodine</subject><subject>Isoelectric Point</subject><subject>Kinetics</subject><subject>Mathematics</subject><subject>Muscle Proteins - metabolism</subject><subject>Other techniques and industries</subject><subject>Parvalbumins - metabolism</subject><subject>Spectrometry, Fluorescence</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1985</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kM2qFDEQRoMo1_HqGyj0QkQXrZVOOp1sBLn4Bxd0oSsXoZKuQKS7MybdA_P2Zpxhlq6K4jtVfBzGnnN4y4GrdwAgWqMVf637NwZAD616wHYcjGpBaPmQ7a7IY_aklN8AnEvV3bAbYbpBS7Fjv75jPuDktjkujU9LSHmmXJpMB8KJxsYdm7ISjse2rLhSg8vYrHGmNlNJ06ESYdpSXTwtnpqyJ7_mVHzaH5-yRwGnQs8u85b9_PTxx92X9v7b5693H-5bL7RaW6_CiFo6J3tQA4EROoRODpIcCjDotendKPouuEEoNCgEd8BJuBoCd-KWvTr_3ef0Z6Oy2jnWOtOEC6Wt2EF10iipKyjPoK8NS6Zg9znOmI-Wgz05tSdh9iTM6t7-c2pVPXtx-b-5mcbr0UVizV9eciwep5Bx8bFcMa0lVLBi788YVReHSNkWH0_SxpirNDum-P8efwGczpRC</recordid><startdate>19850801</startdate><enddate>19850801</enddate><creator>Permyakov, E.A.</creator><creator>Ostrovsky, A.V.</creator><creator>Burstein, E.A.</creator><creator>Pleshanov, P.G.</creator><creator>Gerday, Ch</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>19850801</creationdate><title>Parvalbumin conformers revealed by steady-state and time-resolved fluorescence spectroscopy</title><author>Permyakov, E.A. ; Ostrovsky, A.V. ; Burstein, E.A. ; Pleshanov, P.G. ; Gerday, Ch</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c386t-c6fda84bb45067e0938ff2474eba309ac895bd352fb736a9a331b01e3b09a01b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1985</creationdate><topic>Animals</topic><topic>Applied sciences</topic><topic>Calcium - metabolism</topic><topic>Egtazic Acid</topic><topic>Exact sciences and technology</topic><topic>Fishes - metabolism</topic><topic>Iodine</topic><topic>Isoelectric Point</topic><topic>Kinetics</topic><topic>Mathematics</topic><topic>Muscle Proteins - metabolism</topic><topic>Other techniques and industries</topic><topic>Parvalbumins - metabolism</topic><topic>Spectrometry, Fluorescence</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Permyakov, E.A.</creatorcontrib><creatorcontrib>Ostrovsky, A.V.</creatorcontrib><creatorcontrib>Burstein, E.A.</creatorcontrib><creatorcontrib>Pleshanov, P.G.</creatorcontrib><creatorcontrib>Gerday, Ch</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>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Permyakov, E.A.</au><au>Ostrovsky, A.V.</au><au>Burstein, E.A.</au><au>Pleshanov, P.G.</au><au>Gerday, Ch</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Parvalbumin conformers revealed by steady-state and time-resolved fluorescence spectroscopy</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1985-08-01</date><risdate>1985</risdate><volume>240</volume><issue>2</issue><spage>781</spage><epage>791</epage><pages>781-791</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><coden>ABBIA4</coden><abstract>The binding of calcium to whiting (one tryptophan residue) and pike (one tyrosine residue) parvalbumins has been studied by means of kinetic and steady-state fluorescence techniques. The decay curves of the tryptophan and tyrosine fluorescence of the parvalbumins are best fitted by a sum of two exponents for any metal state of the proteins. The data can be interpreted as a nonexponential decay of the fluorescence of a single-type chromophore or in terms of equilibria between compact and relaxed conformers of the parvalbumins in each metal state. Fluorescence quenching by I
− ions and effects of H
20/D
20 substitution confirm the second interpretation. The constants of the equilibria have been evaluated.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>3927843</pmid><doi>10.1016/0003-9861(85)90087-6</doi><tpages>11</tpages></addata></record> |
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| ispartof | Archives of biochemistry and biophysics, 1985-08, Vol.240 (2), p.781-791 |
| issn | 0003-9861 1096-0384 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Animals Applied sciences Calcium - metabolism Egtazic Acid Exact sciences and technology Fishes - metabolism Iodine Isoelectric Point Kinetics Mathematics Muscle Proteins - metabolism Other techniques and industries Parvalbumins - metabolism Spectrometry, Fluorescence |
| title | Parvalbumin conformers revealed by steady-state and time-resolved fluorescence spectroscopy |
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