Peroxidase-like Activity of Glass-Beads Modified with Metal-Porphines and Their Analytical Applications
Peroxidase-like activities of glass-beads modified with metal-porphines (M-PG) were examined through a dye-formation reaction, which was catalyzed by peroxidase, of phenol and 4-aminoantipyrine in the presence of hydrogen peroxide. When M-PG was used as a catalyst in place of peroxidase, glass-beads...
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Veröffentlicht in: | Analytical Sciences 2000, Vol.16(11), pp.1121-1125 |
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description | Peroxidase-like activities of glass-beads modified with metal-porphines (M-PG) were examined through a dye-formation reaction, which was catalyzed by peroxidase, of phenol and 4-aminoantipyrine in the presence of hydrogen peroxide. When M-PG was used as a catalyst in place of peroxidase, glass-beads modified with Mn3+- and Fe3+-tetrakis(4-carboxyphenyl)porphine derivatives (Mn- and Fe-TCPPG) showed relatively strong peroxidase-like activity among the M-PG examined. The percentage of the resulting quinoid dye by Mn- and Fe-TCPPG reached to about 93% and 88%, respectively, of that formed by peroxidase. Peroxidase-like activity of Mn-TCPPG was applied to the determination of hydrogen peroxide in place of peroxidase. Furthermore, the determination of serum compounds (glucose and uric acid), which form hydrogen peroxide by using their oxidases, was examined. |
doi_str_mv | 10.2116/analsci.16.1121 |
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When M-PG was used as a catalyst in place of peroxidase, glass-beads modified with Mn3+- and Fe3+-tetrakis(4-carboxyphenyl)porphine derivatives (Mn- and Fe-TCPPG) showed relatively strong peroxidase-like activity among the M-PG examined. The percentage of the resulting quinoid dye by Mn- and Fe-TCPPG reached to about 93% and 88%, respectively, of that formed by peroxidase. Peroxidase-like activity of Mn-TCPPG was applied to the determination of hydrogen peroxide in place of peroxidase. 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When M-PG was used as a catalyst in place of peroxidase, glass-beads modified with Mn3+- and Fe3+-tetrakis(4-carboxyphenyl)porphine derivatives (Mn- and Fe-TCPPG) showed relatively strong peroxidase-like activity among the M-PG examined. The percentage of the resulting quinoid dye by Mn- and Fe-TCPPG reached to about 93% and 88%, respectively, of that formed by peroxidase. Peroxidase-like activity of Mn-TCPPG was applied to the determination of hydrogen peroxide in place of peroxidase. Furthermore, the determination of serum compounds (glucose and uric acid), which form hydrogen peroxide by using their oxidases, was examined.</description><subject>Analytical biochemistry: general aspects, technics, instrumentation</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Fundamental and applied biological sciences. 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Psychology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>MIFUNE, Masaki</creatorcontrib><creatorcontrib>IWADO, Akimasa</creatorcontrib><creatorcontrib>AKIZAWA, Hiromichi</creatorcontrib><creatorcontrib>SUGIMOTO, Katsuyoshi</creatorcontrib><creatorcontrib>SAITO, Yutaka</creatorcontrib><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Aluminium Industry Abstracts</collection><collection>Biotechnology Research Abstracts</collection><collection>Ceramic Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Copper Technical Reference Library</collection><collection>Materials Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Analytical Sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>MIFUNE, Masaki</au><au>IWADO, Akimasa</au><au>AKIZAWA, Hiromichi</au><au>SUGIMOTO, Katsuyoshi</au><au>SAITO, Yutaka</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Peroxidase-like Activity of Glass-Beads Modified with Metal-Porphines and Their Analytical Applications</atitle><jtitle>Analytical Sciences</jtitle><date>2000-11-01</date><risdate>2000</risdate><volume>16</volume><issue>11</issue><spage>1121</spage><epage>1125</epage><pages>1121-1125</pages><issn>0910-6340</issn><eissn>1348-2246</eissn><coden>ANSCEN</coden><abstract>Peroxidase-like activities of glass-beads modified with metal-porphines (M-PG) were examined through a dye-formation reaction, which was catalyzed by peroxidase, of phenol and 4-aminoantipyrine in the presence of hydrogen peroxide. When M-PG was used as a catalyst in place of peroxidase, glass-beads modified with Mn3+- and Fe3+-tetrakis(4-carboxyphenyl)porphine derivatives (Mn- and Fe-TCPPG) showed relatively strong peroxidase-like activity among the M-PG examined. The percentage of the resulting quinoid dye by Mn- and Fe-TCPPG reached to about 93% and 88%, respectively, of that formed by peroxidase. Peroxidase-like activity of Mn-TCPPG was applied to the determination of hydrogen peroxide in place of peroxidase. Furthermore, the determination of serum compounds (glucose and uric acid), which form hydrogen peroxide by using their oxidases, was examined.</abstract><cop>Tokyo</cop><pub>The Japan Society for Analytical Chemistry</pub><doi>10.2116/analsci.16.1121</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Analytical biochemistry: general aspects, technics, instrumentation Analytical, structural and metabolic biochemistry Biological and medical sciences Fundamental and applied biological sciences. Psychology |
title | Peroxidase-like Activity of Glass-Beads Modified with Metal-Porphines and Their Analytical Applications |
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