PREPARATION AND PROPERTIES OF HORSERADISH PEROXIDASE CROSS-LINKED IN NONAQUEOUS MEDIA
Horseradish peroxidase (hydrogen peroxide oxidoreductase [1.11.1.7]) has been cross‐linked in methylene chloride using N,N'‐carbonyldiimidazole to produce a water insoluble preparation which retains enzymatic activity. Relative to native enzyme, which was treated with methylene chloride but not...
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Veröffentlicht in: | International Journal of Peptide and Protein Research 1974-09, Vol.6 (5), p.287-294 |
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container_title | International Journal of Peptide and Protein Research |
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creator | Bartling, Greg J. Chattopadhyay, Swaraj K. Barker, Charles W. Forrester, Lawrence J. Brown, Harry D. |
description | Horseradish peroxidase (hydrogen peroxide oxidoreductase [1.11.1.7]) has been cross‐linked in methylene chloride using N,N'‐carbonyldiimidazole to produce a water insoluble preparation which retains enzymatic activity. Relative to native enzyme, which was treated with methylene chloride but not N,N'‐carbonyldiimidazole, the cross‐linked product displayed significant stability toward denaturation in aqueous mixtures of ethanol, methanol, and 1,4‐dioxane. The cross‐linked product showed a a marked stability toward thermal denaturation relative to the native protein. Applications of the catalyst in chemical reactors for the preparation of synthetic quinones are discussed. |
doi_str_mv | 10.1111/j.1399-3011.1974.tb02387.x |
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Relative to native enzyme, which was treated with methylene chloride but not N,N'‐carbonyldiimidazole, the cross‐linked product displayed significant stability toward denaturation in aqueous mixtures of ethanol, methanol, and 1,4‐dioxane. The cross‐linked product showed a a marked stability toward thermal denaturation relative to the native protein. 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Relative to native enzyme, which was treated with methylene chloride but not N,N'‐carbonyldiimidazole, the cross‐linked product displayed significant stability toward denaturation in aqueous mixtures of ethanol, methanol, and 1,4‐dioxane. The cross‐linked product showed a a marked stability toward thermal denaturation relative to the native protein. Applications of the catalyst in chemical reactors for the preparation of synthetic quinones are discussed.</description><subject>Depression, Chemical</subject><subject>Dioxanes - pharmacology</subject><subject>Ethanol - pharmacology</subject><subject>Hydrocarbons, Chlorinated - pharmacology</subject><subject>Imidazoles</subject><subject>In Vitro Techniques</subject><subject>Iron - analysis</subject><subject>Methanol - pharmacology</subject><subject>Peroxidases - analysis</subject><subject>Peroxidases - chemical synthesis</subject><subject>Peroxidases - metabolism</subject><subject>Protein Denaturation - drug effects</subject><subject>Solubility</subject><subject>Solutions</subject><subject>Solvents</subject><subject>Spectrophotometry</subject><subject>Spectrophotometry, Infrared</subject><subject>Spectrum Analysis</subject><subject>Temperature</subject><subject>Time Factors</subject><issn>0367-8377</issn><issn>1399-3011</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1974</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkFFv2jAQx61pU0e7foRJ1h72ltT2JdjZy5QSF6KyOE1g25vlJI4Eg9HFoNJv30Qg3ncvJ93_7mf5h9AXSnza193apxBFHhBKfRrxwN9XhIHg_vEdGl2i92hEYMw9AZx_RNfOrQmBADi7QldBACQM-Qgt80LmcREvUpXhOEtwXqhcFotUllg94JkqSlnESVrOcD9Wv9MkLiWeFKosvXmaPcoEpxnOVBY_LaValviHTNL4E_rQmo2zt-d-g5YPcjGZeXM1TSfx3KuBAfeqoGqpbUwkLBPUGFFTA6RtTWjCUDS0JkEwBhbxEIjh0ESiH4swqmzDgrpt4AZ9PXGfu92_g3V7vV252m425q_dHZwWrP8k4aJf_HZarLudc51t9XO32pruVVOiB6d6rQdxehCnB6f67FQf--PP51cO1dY2l9OzxD7_fspfVhv7-h9kPblPEiYGgncirNzeHi8E0_3RYw481L-yqZ4-snxGFvf6J7wBxleOVQ</recordid><startdate>197409</startdate><enddate>197409</enddate><creator>Bartling, Greg J.</creator><creator>Chattopadhyay, Swaraj K.</creator><creator>Barker, Charles W.</creator><creator>Forrester, Lawrence J.</creator><creator>Brown, Harry D.</creator><general>Blackwell Publishing Ltd</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>7X8</scope></search><sort><creationdate>197409</creationdate><title>PREPARATION AND PROPERTIES OF HORSERADISH PEROXIDASE CROSS-LINKED IN NONAQUEOUS MEDIA</title><author>Bartling, Greg J. ; Chattopadhyay, Swaraj K. ; Barker, Charles W. ; Forrester, Lawrence J. ; Brown, Harry D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3237-b4bf1eda98e281aa8c1a30ffa5a558d1c04463297530a73d98558859bed24cfd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1974</creationdate><topic>Depression, Chemical</topic><topic>Dioxanes - pharmacology</topic><topic>Ethanol - pharmacology</topic><topic>Hydrocarbons, Chlorinated - pharmacology</topic><topic>Imidazoles</topic><topic>In Vitro Techniques</topic><topic>Iron - analysis</topic><topic>Methanol - pharmacology</topic><topic>Peroxidases - analysis</topic><topic>Peroxidases - chemical synthesis</topic><topic>Peroxidases - metabolism</topic><topic>Protein Denaturation - drug effects</topic><topic>Solubility</topic><topic>Solutions</topic><topic>Solvents</topic><topic>Spectrophotometry</topic><topic>Spectrophotometry, Infrared</topic><topic>Spectrum Analysis</topic><topic>Temperature</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bartling, Greg J.</creatorcontrib><creatorcontrib>Chattopadhyay, Swaraj K.</creatorcontrib><creatorcontrib>Barker, Charles W.</creatorcontrib><creatorcontrib>Forrester, Lawrence J.</creatorcontrib><creatorcontrib>Brown, Harry D.</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>MEDLINE - Academic</collection><jtitle>International Journal of Peptide and Protein Research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bartling, Greg J.</au><au>Chattopadhyay, Swaraj K.</au><au>Barker, Charles W.</au><au>Forrester, Lawrence J.</au><au>Brown, Harry D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>PREPARATION AND PROPERTIES OF HORSERADISH PEROXIDASE CROSS-LINKED IN NONAQUEOUS MEDIA</atitle><jtitle>International Journal of Peptide and Protein Research</jtitle><addtitle>Int J Pept Protein Res</addtitle><date>1974-09</date><risdate>1974</risdate><volume>6</volume><issue>5</issue><spage>287</spage><epage>294</epage><pages>287-294</pages><issn>0367-8377</issn><eissn>1399-3011</eissn><abstract>Horseradish peroxidase (hydrogen peroxide oxidoreductase [1.11.1.7]) has been cross‐linked in methylene chloride using N,N'‐carbonyldiimidazole to produce a water insoluble preparation which retains enzymatic activity. Relative to native enzyme, which was treated with methylene chloride but not N,N'‐carbonyldiimidazole, the cross‐linked product displayed significant stability toward denaturation in aqueous mixtures of ethanol, methanol, and 1,4‐dioxane. The cross‐linked product showed a a marked stability toward thermal denaturation relative to the native protein. Applications of the catalyst in chemical reactors for the preparation of synthetic quinones are discussed.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>4430557</pmid><doi>10.1111/j.1399-3011.1974.tb02387.x</doi><tpages>8</tpages></addata></record> |
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subjects | Depression, Chemical Dioxanes - pharmacology Ethanol - pharmacology Hydrocarbons, Chlorinated - pharmacology Imidazoles In Vitro Techniques Iron - analysis Methanol - pharmacology Peroxidases - analysis Peroxidases - chemical synthesis Peroxidases - metabolism Protein Denaturation - drug effects Solubility Solutions Solvents Spectrophotometry Spectrophotometry, Infrared Spectrum Analysis Temperature Time Factors |
title | PREPARATION AND PROPERTIES OF HORSERADISH PEROXIDASE CROSS-LINKED IN NONAQUEOUS MEDIA |
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