Purification and characterization of the vanadium bromoperoxidase from the macroalga Corallina officinalis
The red macroalga Corallina officinalis contains a bromoperoxidase whose activity is vanadium-dependent. This enzyme has been purified to homogeneity as judged from non-denaturing PAGE and SDS-PAGE. Sedimentation equilibrium studies gave a value for Mr of 740 000, whereas a Mr of 64 000 was obtained...
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| Veröffentlicht in: | Phytochemistry (Oxford) 1993, Vol.32 (1), p.21-26 |
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| creator | Sheffield, D.J Harry, T Smith, A.J Rogers, L.J |
| description | The red macroalga Corallina officinalis contains a bromoperoxidase whose activity is vanadium-dependent. This enzyme has been purified to homogeneity as judged from non-denaturing PAGE and SDS-PAGE. Sedimentation equilibrium studies gave a value for Mr of 740 000, whereas a Mr of 64 000 was obtained by SDS-PAGE. The native enzyme thus appears to be an oligomer, probably of 12 identical subunits. Kinetic studies for the bromination of monochlorodimedone (MCD) gave the following: Km(Br-), 1.0 mM; Km(H2O2), 60 micromolar and Km(MCD), 21 micromolar. The bromoperoxidase showed remarkable thermostability, retaining appreciable activity at 60-70 degrees and recovering the original activity on re-equilibration to 25 degrees, even on repeated cycles of this temperature regime. The enzyme also showed tolerance to a range of organic solvents and chaotropic agents. |
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This enzyme has been purified to homogeneity as judged from non-denaturing PAGE and SDS-PAGE. Sedimentation equilibrium studies gave a value for Mr of 740 000, whereas a Mr of 64 000 was obtained by SDS-PAGE. The native enzyme thus appears to be an oligomer, probably of 12 identical subunits. Kinetic studies for the bromination of monochlorodimedone (MCD) gave the following: Km(Br-), 1.0 mM; Km(H2O2), 60 micromolar and Km(MCD), 21 micromolar. The bromoperoxidase showed remarkable thermostability, retaining appreciable activity at 60-70 degrees and recovering the original activity on re-equilibration to 25 degrees, even on repeated cycles of this temperature regime. The enzyme also showed tolerance to a range of organic solvents and chaotropic agents.</description><identifier>ISSN: 0031-9422</identifier><identifier>EISSN: 1873-3700</identifier><language>eng</language><publisher>Amsterdam: Elsevier</publisher><subject>algae ; Biological and medical sciences ; bromides ; bromine ; bromoperoxidase ; characterization ; chemical analysis ; chemical constituents of plants ; Corallina officinalis ; enzyme activity ; Enzymes ; Fundamental and applied biological sciences. Psychology ; halogen compounds ; kinetics ; Marine ; Metabolism ; peroxidase ; Plant physiology and development ; purification ; regulation ; Rhodophycota ; Rhodophyta ; seaweeds ; substrates ; vanadium ; vanadium bromoperoxidase</subject><ispartof>Phytochemistry (Oxford), 1993, Vol.32 (1), p.21-26</ispartof><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,778,782,4012</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4700560$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Sheffield, D.J</creatorcontrib><creatorcontrib>Harry, T</creatorcontrib><creatorcontrib>Smith, A.J</creatorcontrib><creatorcontrib>Rogers, L.J</creatorcontrib><title>Purification and characterization of the vanadium bromoperoxidase from the macroalga Corallina officinalis</title><title>Phytochemistry (Oxford)</title><description>The red macroalga Corallina officinalis contains a bromoperoxidase whose activity is vanadium-dependent. This enzyme has been purified to homogeneity as judged from non-denaturing PAGE and SDS-PAGE. Sedimentation equilibrium studies gave a value for Mr of 740 000, whereas a Mr of 64 000 was obtained by SDS-PAGE. The native enzyme thus appears to be an oligomer, probably of 12 identical subunits. Kinetic studies for the bromination of monochlorodimedone (MCD) gave the following: Km(Br-), 1.0 mM; Km(H2O2), 60 micromolar and Km(MCD), 21 micromolar. The bromoperoxidase showed remarkable thermostability, retaining appreciable activity at 60-70 degrees and recovering the original activity on re-equilibration to 25 degrees, even on repeated cycles of this temperature regime. The enzyme also showed tolerance to a range of organic solvents and chaotropic agents.</description><subject>algae</subject><subject>Biological and medical sciences</subject><subject>bromides</subject><subject>bromine</subject><subject>bromoperoxidase</subject><subject>characterization</subject><subject>chemical analysis</subject><subject>chemical constituents of plants</subject><subject>Corallina officinalis</subject><subject>enzyme activity</subject><subject>Enzymes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>halogen compounds</subject><subject>kinetics</subject><subject>Marine</subject><subject>Metabolism</subject><subject>peroxidase</subject><subject>Plant physiology and development</subject><subject>purification</subject><subject>regulation</subject><subject>Rhodophycota</subject><subject>Rhodophyta</subject><subject>seaweeds</subject><subject>substrates</subject><subject>vanadium</subject><subject>vanadium bromoperoxidase</subject><issn>0031-9422</issn><issn>1873-3700</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><recordid>eNotkE1LxDAQhosouK7-BnsQb4VJmqTNURa_YEFB91wmabKbJW3WpBX111vtnmbe4Xmfw5xkC1JXZVFWAKfZAqAkhWSUnmcXKe0BgHMhFtn-dYzOOo2DC32OfZvrHUbUg4nuZz4Gmw87k39ij60bu1zF0IWDieHLtZhMbqf8T3SoY0C_xXwVInrvepzKk3xavEuX2ZlFn8zVcS6zzcP9--qpWL88Pq_u1oUlQg4FagmKSiqJki1IQ6liSJjmqGpGJOMVa8FSWylNACwrhRGgtFHEGMsJlMvsdvYeYvgYTRqaziVtvMfehDE1RHBZcSYn8OYIYtLobcReu9Qcouswfjds-hwXf77rGbMYGtzGCdm8USAlkKqmpBblL2JUbjE</recordid><startdate>1993</startdate><enddate>1993</enddate><creator>Sheffield, D.J</creator><creator>Harry, T</creator><creator>Smith, A.J</creator><creator>Rogers, L.J</creator><general>Elsevier</general><scope>FBQ</scope><scope>IQODW</scope><scope>7QL</scope><scope>7TN</scope><scope>8FD</scope><scope>C1K</scope><scope>F1W</scope><scope>FR3</scope><scope>H95</scope><scope>H99</scope><scope>L.F</scope><scope>L.G</scope><scope>M7N</scope><scope>M81</scope><scope>P64</scope></search><sort><creationdate>1993</creationdate><title>Purification and characterization of the vanadium bromoperoxidase from the macroalga Corallina officinalis</title><author>Sheffield, D.J ; Harry, T ; Smith, A.J ; Rogers, L.J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-f169t-ac90b29291b9d09e22b4a14c5ab84194574d0f2f7bc100f436e60bceb1eef5103</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>algae</topic><topic>Biological and medical sciences</topic><topic>bromides</topic><topic>bromine</topic><topic>bromoperoxidase</topic><topic>characterization</topic><topic>chemical analysis</topic><topic>chemical constituents of plants</topic><topic>Corallina officinalis</topic><topic>enzyme activity</topic><topic>Enzymes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>halogen compounds</topic><topic>kinetics</topic><topic>Marine</topic><topic>Metabolism</topic><topic>peroxidase</topic><topic>Plant physiology and development</topic><topic>purification</topic><topic>regulation</topic><topic>Rhodophycota</topic><topic>Rhodophyta</topic><topic>seaweeds</topic><topic>substrates</topic><topic>vanadium</topic><topic>vanadium bromoperoxidase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sheffield, D.J</creatorcontrib><creatorcontrib>Harry, T</creatorcontrib><creatorcontrib>Smith, A.J</creatorcontrib><creatorcontrib>Rogers, L.J</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Oceanic Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>ASFA: Marine Biotechnology Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Marine Biotechnology Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Phytochemistry (Oxford)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sheffield, D.J</au><au>Harry, T</au><au>Smith, A.J</au><au>Rogers, L.J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and characterization of the vanadium bromoperoxidase from the macroalga Corallina officinalis</atitle><jtitle>Phytochemistry (Oxford)</jtitle><date>1993</date><risdate>1993</risdate><volume>32</volume><issue>1</issue><spage>21</spage><epage>26</epage><pages>21-26</pages><issn>0031-9422</issn><eissn>1873-3700</eissn><abstract>The red macroalga Corallina officinalis contains a bromoperoxidase whose activity is vanadium-dependent. This enzyme has been purified to homogeneity as judged from non-denaturing PAGE and SDS-PAGE. Sedimentation equilibrium studies gave a value for Mr of 740 000, whereas a Mr of 64 000 was obtained by SDS-PAGE. The native enzyme thus appears to be an oligomer, probably of 12 identical subunits. Kinetic studies for the bromination of monochlorodimedone (MCD) gave the following: Km(Br-), 1.0 mM; Km(H2O2), 60 micromolar and Km(MCD), 21 micromolar. The bromoperoxidase showed remarkable thermostability, retaining appreciable activity at 60-70 degrees and recovering the original activity on re-equilibration to 25 degrees, even on repeated cycles of this temperature regime. The enzyme also showed tolerance to a range of organic solvents and chaotropic agents.</abstract><cop>Amsterdam</cop><pub>Elsevier</pub><tpages>6</tpages></addata></record> |
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| ispartof | Phytochemistry (Oxford), 1993, Vol.32 (1), p.21-26 |
| issn | 0031-9422 1873-3700 |
| language | eng |
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| source | Elsevier ScienceDirect Journals Complete - AutoHoldings |
| subjects | algae Biological and medical sciences bromides bromine bromoperoxidase characterization chemical analysis chemical constituents of plants Corallina officinalis enzyme activity Enzymes Fundamental and applied biological sciences. Psychology halogen compounds kinetics Marine Metabolism peroxidase Plant physiology and development purification regulation Rhodophycota Rhodophyta seaweeds substrates vanadium vanadium bromoperoxidase |
| title | Purification and characterization of the vanadium bromoperoxidase from the macroalga Corallina officinalis |
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