The oxidation of naphthalene sulfonate dyes by horse radish peroxidase
Horse radish peroxidase catalyses oxidation of ANS and TNS with hydrogen peroxide. TNS peroxidation may be followed fluorimetrically in the presence of as low as 10 −12 m concentrations of the enzyme and permits determination of very low levels of peroxides. Initial rates of peroxidation of ANS and...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 1982-01, Vol.217 (2), p.529-535 |
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| container_end_page | 535 |
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| container_issue | 2 |
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| container_title | Archives of biochemistry and biophysics |
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| creator | Sasson, Lydia Sharabani, Michaela Aviram, Irit |
| description | Horse radish peroxidase catalyses oxidation of ANS and TNS with hydrogen peroxide. TNS peroxidation may be followed fluorimetrically in the presence of as low as 10
−12
m concentrations of the enzyme and permits determination of very low levels of peroxides. Initial rates of peroxidation of ANS and TNS confirmed the general mechanism of peroxidation by HRP. The second-order rate constants for the reduction of HRP compounds I and II were determined. Binding of the substrates to hydrophobic sites of bovine serum albumin or apoperoxidase rendered them inaccessible to the enzyme. While benzhydroxamic acid inhibited the oxidation of dianisidine, it exerted an activating effect on the peroxidation of naphthalene sulfonates. Due to the high reactivity of naphthalene sulfonates, their application as probes in biological systems containing possible traces of peroxidases and peroxides should be interpreted with great caution. |
| doi_str_mv | 10.1016/0003-9861(82)90534-3 |
| format | Article |
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−12
m concentrations of the enzyme and permits determination of very low levels of peroxides. Initial rates of peroxidation of ANS and TNS confirmed the general mechanism of peroxidation by HRP. The second-order rate constants for the reduction of HRP compounds I and II were determined. Binding of the substrates to hydrophobic sites of bovine serum albumin or apoperoxidase rendered them inaccessible to the enzyme. While benzhydroxamic acid inhibited the oxidation of dianisidine, it exerted an activating effect on the peroxidation of naphthalene sulfonates. Due to the high reactivity of naphthalene sulfonates, their application as probes in biological systems containing possible traces of peroxidases and peroxides should be interpreted with great caution.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/0003-9861(82)90534-3</identifier><identifier>PMID: 7138023</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Coloring Agents ; Horseradish Peroxidase - metabolism ; Hydrogen-Ion Concentration ; Kinetics ; Naphthalenesulfonates ; Oxidation-Reduction ; Peroxidases - metabolism ; plant biochemistry ; plant physiology ; Spectrometry, Fluorescence</subject><ispartof>Archives of biochemistry and biophysics, 1982-01, Vol.217 (2), p.529-535</ispartof><rights>1982</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c381t-1f66af57256069770f9fa9b794f6b285130ab6a2f499f68b351cdf2955a9ea993</citedby><cites>FETCH-LOGICAL-c381t-1f66af57256069770f9fa9b794f6b285130ab6a2f499f68b351cdf2955a9ea993</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0003986182905343$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7138023$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sasson, Lydia</creatorcontrib><creatorcontrib>Sharabani, Michaela</creatorcontrib><creatorcontrib>Aviram, Irit</creatorcontrib><title>The oxidation of naphthalene sulfonate dyes by horse radish peroxidase</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>Horse radish peroxidase catalyses oxidation of ANS and TNS with hydrogen peroxide. TNS peroxidation may be followed fluorimetrically in the presence of as low as 10
−12
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−12
m concentrations of the enzyme and permits determination of very low levels of peroxides. Initial rates of peroxidation of ANS and TNS confirmed the general mechanism of peroxidation by HRP. The second-order rate constants for the reduction of HRP compounds I and II were determined. Binding of the substrates to hydrophobic sites of bovine serum albumin or apoperoxidase rendered them inaccessible to the enzyme. While benzhydroxamic acid inhibited the oxidation of dianisidine, it exerted an activating effect on the peroxidation of naphthalene sulfonates. Due to the high reactivity of naphthalene sulfonates, their application as probes in biological systems containing possible traces of peroxidases and peroxides should be interpreted with great caution.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>7138023</pmid><doi>10.1016/0003-9861(82)90534-3</doi><tpages>7</tpages></addata></record> |
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| identifier | ISSN: 0003-9861 |
| ispartof | Archives of biochemistry and biophysics, 1982-01, Vol.217 (2), p.529-535 |
| issn | 0003-9861 1096-0384 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Coloring Agents Horseradish Peroxidase - metabolism Hydrogen-Ion Concentration Kinetics Naphthalenesulfonates Oxidation-Reduction Peroxidases - metabolism plant biochemistry plant physiology Spectrometry, Fluorescence |
| title | The oxidation of naphthalene sulfonate dyes by horse radish peroxidase |
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