Determination of hydrogen peroxide with N,N-diethylaniline and 4-aminoantipyrine by use of an anion-exchange resin modified with manganese-tetrakis(sulphophenyl)porphine, as a substitute for peroxidase

Saito, Yutaka; Mifune, Masaki; Nakashima, Suzuyo; Odo, Junichi; Tanaka, Yoshimasa; Chikuma, Masahiko; Tanaka, Hisashi

doi:10.1016/0039-9140(87)80086-3

Cited by 56 publications

(29 citation statements)

References 4 publications

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“…Therefore, the study of potential alternatives is one of the interesting trends in analytical biochemistry. Several metal-porphyrin [23][24][25] and metalphthalocyanine 12,26 complexes, hemin 27 and β-CD-hemin 28,29 have been used as mimetic enzymes instead of POx for the determination of H2O2. In recent years the use of plant tissue materials and crude extracts of various vegetables as novel biocatalysts has also received considerable interest for replacing isolated enzymes.…”

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confidence: 99%

Application of Crude Extract of Kohlrabi (Brassica oleracea gongylodes) as a Rich Source of Peroxidase in the Spectrofluorometric Determination of Hydrogen Peroxide in Honey Samples

2006

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Crude extract of kohlrabi (Brassica oleracea gongylodes) was prepared by a simple procedure and its enzymatic activity and total protein concentration were determined. It was found that this crude extract is a rich source of peroxidase (POx) and has high specific activity. Cross-linked polyvinylpyrrolidone was used as a stabilizer in the preparation of the crude extract. The POx activity of kohlrabi crude extract did not vary for at least 2 months when deoxygenated and stored at 4˚C. This extract was applied for the spectrofluorometric determination of hydrogen peroxide using homovanillic acid as a fluorogenic substrate. POx catalyzes the hydrogen peroxide oxidation of homovanillic acid to produce a dimer which shows strong fluorescence at 420 nm with excitation at 312 nm. In the optimum conditions, the calibration graph for hydrogen peroxide was linear up to 190 ng mL -1 , with a detection limit of 4.4 ng mL -1 . The relative standard deviation (RSD) was 1.48% for 50 ng mL -1 hydrogen peroxide. The proposed method was successfully applied to the determination of hydrogen peroxide in honey. The concentration-time profile of H2O2 produced upon dilution of honey was studied and H2O2 contents of some different honeys from various areas of Iran were determined.

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Application of Crude Extract of Kohlrabi (Brassica oleracea gongylodes) as a Rich Source of Peroxidase in the Spectrofluorometric Determination of Hydrogen Peroxide in Honey Samples

2006

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“…As a study of improvement of these disadvantages, it was previously indicated that some resins modified with metallo-porphyrins exhibit such enzyme-like activities as peroxidase, catalase and uricase, and are available for clinical analyses as good mimics of these enzymes. [2][3][4][5] In the present study resins modified with Mn3+-tetrakis(4-sulfophenyl)porphine and Mn3+-tetrakis(1-methylpyridinium-4-yl)porphine, exhibiting a uricaselike catalytic activity, were dealt with by means of resonance Raman spectroscopy. In order to know how these modified resins act as a catalyst, the resonance Raman spectra were measured in the course of oxidizing uric acid.…”

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Resonance Raman Spectra of Manganese-Porphyrins on Ion-Exchange Resins Exhibiting Uricase-Like Catalytic Activity

et al. 1991

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Ion-exchange resins modified with some manganese(III)-porphyrins (Mn3+-Pr) show a uricase-like catalytic activity, which is applicable to the determination of uric acid. The resonance Raman spectra of Mn3+-Pr indicate that Mn3+-porphyrins on modified resins are reduced to Mn2+-porphyrins with oxidizing uric acid; Mn2+-porphyrins then return to Mn3+-porphyrins by oxidation with 02 in the reaction system. It was concluded on the basis of these results that the modified resins show an uricase-like activity by repeating this redox cycle of manganese-porphyrins on the modified resins. Mn3+-Pr exhibited no oxidative catalytic activity for 7-methylated derivatives of uric acid, indicating that the nitrogen atom at the 7-position of uric acid plays an important role in the activity of Mn3+-Pr. In clinical assays, enzyme reactions catalyzed by uricase, peroxidase and catalase are frequently used as important analytical reactions. However, these enzymes have some disadvantages regarding stability, handling, purity and storage. As a study of improvement of these disadvantages, it was previously indicated that some resins modified with metallo-porphyrins exhibit such enzyme-like activities as peroxidase, catalase and uricase, and are available for clinical analyses as good mimics of these enzymes.2-5In the present study resins modified with Mn3+-tetrakis(4-sulfophenyl)porphine and Mn3+-tetrakis(1-methylpyridinium-4-yl)porphine, exhibiting a uricaselike catalytic activity, were dealt with by means of resonance Raman spectroscopy. In order to know how these modified resins act as a catalyst, the resonance Raman spectra were measured in the course of oxidizing uric acid. As the result, the uricase-like activity of the modified resins was found to be caused by a redox cycle of manganese ion. Experimental CompoundsTetrakis(4-sulfophenyl)porphine (TPPS) and tetrakis(1-methylpyridinium-4-yl)porphine (TMPyP) were purchased from Tokyo Kasei Kogyo Co. Ltd. and used without further purification. Their manganese(III)-complexes, Mn3+-TPPS and Mn3+-TMPyP (Fig. 1), were prepared by methods similar to those given in the literature.6 Anion-exchange (Amberlite IRA 900) and a cation-exchange (Dowex MSC-1) resins were regenerated in their chloride and sodium forms, respectively. The resins modified with manganese-porphyrins (25 µmol/ g), Mn3+-TPPSr and Mn3+-TMPyPr, were prepared as described before.6 All other chemicals were of reagent grade and used without further purification. Stock solutions of the samples were prepared by dissolving uric acid (UA) or its derivatives (0.1 g, Sigma Chemical Co.) with lithium carbonate (0.1 g) in 100 ml water. A buffer solution (pH 11.0) was prepared by mixing a 0.2 M sodium carbonate solution with a 0.2 M boric acid-0.2 M potassium chloride solution.t Present address:

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“…[8][9][10][11][12][13] The resultant Cu-PCS r (20 -500 µmol Cu-PCS/g dry MSA-1) was filtered, washed with water and then acetone, and dried under vacuum to obtain the Cu-PCS r . All the modified resins were stable against temperature, moisture and storage.…”

Section: Preparation Of Msa-1 Modified With Cu-pcs (Cu-pcs R )mentioning

confidence: 99%

Separation of π-Electron-Rich Compounds by Using Anion-Exchange Resin Modified with Cu2+-Phthalocyanine Derivative as Stationary Phase for Chromatography

et al. 1999

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Recently, many HPLC stationary phases mainly based on π-π electron interaction (π-π interaction) have been developed for the separation of π-electron-rich compounds. Those include silica gels binding Cu 2+ -phthalocyanine 1-3 and In 3+ -porphine 4,5 and pyrene 6,7 derivatives. However, the preparation of such silica gels requires troublesome procedures 2,4,6 and the base silica gels for HPLC are relatively expensive. On the other hand, we have found that anionic metal-porphines are easily fastened on an ordinary anion-exchange resin through electrostatic and hydrophobic interactions. 8-13These facts led us to develop a stationary phase by modifying an anion-exchange resin with anionic Cu 2+ -phthalocyanine derivative (Cu-PCS r ), which would be prepared easily and cheaply. In the present paper, we would like to report briefly the utility of the resultant resin (hereinafter referred to as Cu-PCS r ) as a stationary phase for the separation of π-electron-rich compounds.

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Determination of hydrogen peroxide with N,N-diethylaniline and 4-aminoantipyrine by use of an anion-exchange resin modified with manganese-tetrakis(sulphophenyl)porphine, as a substitute for peroxidase

Cited by 56 publications

References 4 publications

Application of Crude Extract of Kohlrabi (Brassica oleracea gongylodes) as a Rich Source of Peroxidase in the Spectrofluorometric Determination of Hydrogen Peroxide in Honey Samples

Application of Crude Extract of Kohlrabi (Brassica oleracea gongylodes) as a Rich Source of Peroxidase in the Spectrofluorometric Determination of Hydrogen Peroxide in Honey Samples

Resonance Raman Spectra of Manganese-Porphyrins on Ion-Exchange Resins Exhibiting Uricase-Like Catalytic Activity

Separation of π-Electron-Rich Compounds by Using Anion-Exchange Resin Modified with Cu2+-Phthalocyanine Derivative as Stationary Phase for Chromatography

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