Chemical analysis for small amounts of horseradish peroxidase using “porphyrinogen” as a chromogenic reagent

Manaka, Atsushi; Sakai, Mutuko; Igarashi, Shukuro

doi:10.1016/s0003-2670(02)01437-x

Cited by 5 publications

(5 citation statements)

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“…[1][2][3][4][5][6][7][8][9] In addition, metal-porphyrin complexes have various functions that are useful in analytical chemistry, and are also of interest to many other researchers, which has led to the use of metal-porphyrin complexes in applications such as optics, 10 chemical stacking, 11 catalysis, 12 electron transport, 13 oxidation-reduction reactions, 14 and biological mimicking substances. 15,16 Thus, numerous reports regarding the chemical function and applications of porphyrin derivatives have been published.…”

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confidence: 99%

β-Cyclodextrin as a Metal-anionic Porphyrin Complexation Accelerator in Aqueous Media

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β-Cyclodextrin as a Metal-anionic Porphyrin Complexation Accelerator in Aqueous Media

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“…Porphyrins, a class of tetrapyrrolic dyes, play a key role in the biochemical processes [20] and are widely used in the chemical analysis as chromogenic reagents [21,22].…”

Section: Introductionmentioning

confidence: 99%

Investigation on the effect of water on the spectroscopic behaviors of TPPS in acidic imidazolium-based ionic liquids

Liu

Zhao

Jin

2012

J. Porphyrins Phthalocyanines

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The effect of water on the spectroscopic behaviors of meso-tetrakis-(4-sulfonatophenyl) porphyrin (TPPS) in acidic 1-butyl-3-methylimidazolium tetrafluoroborate (BMIMBF 4 ) and 1-ethyl-3methylimidazolium tetrafluoroborate (EMIMBF 4 ) is investigated by spectroscopic methods. In acidic ionic liquids without water, the Soret bands of the protonated form (H 4 TPPS 2-) and J-aggregates of TPPS are centered at 449 and 469 nm, respectively, and the Q-band is centered at 679 nm. When increasing the content of water, the Soret band of H 4 TPPS 2is blue-shifted to 430 nm. However, the Soret and Q-bands of J-aggregates are red-shifted to 487 and 701 nm, respectively. The NMR and pyrene-scale polarity experiments reveal that the change of the bulk environment is responsible for the red-shift of J-aggregates and the blue-shift of H 4 TPPS 2-. According to the analysis of the fluorescence spectra, the content of H 4 TPPS 2increases gradually with the addition of water, while the content of H 2 TPPS 4takes the opposite trend. Simultaneously, the content of J-aggregates decreases substantially when the addition of water is 0 ~ ca. 12 mL (or 13 mL) but it decreases slowly with further addition of water. Remarkably, the fluorescence intensity of J-aggregates is relatively strong. In addition, the fluorescence of J-aggregates can be detected when λ ex is set at both λ ex for TPPS monomers and λ ex for J-aggregates. While the fluorescence of TPPS monomers can be detected only when λ ex is set at λ ex for monomers. Moreover, with the addition of water, the fluorescence lifetimes of H 2 TPPS 4and H 4 TPPS 2increase from 3.202 and 0.830 ns to 9.623 and 2.964 ns, respectively.

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“…The sensitivity of spectrophotometry can be improved by combination with heme protein enzymatic activity for the oxidation of chromogens with hydrogen peroxide. 7,8 Unfortunately, it often suffers from interference. In most biological studies, the release of cytochrome c is determined by immunochemical methods.…”

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confidence: 99%

“…8.0 mg L -1 cytochrome c in pH 9.6 NaHCO 3 -Na 2 CO 3 solution; other conditions the same as in Figure1.…”

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confidence: 99%

“…Spectrophotometry has been frequently used for determining cytochrome c release from isolated mitochondria. , It is rapid and simple but is insensitive. The sensitivity of spectrophotometry can be improved by combination with heme protein enzymatic activity for the oxidation of chromogens with hydrogen peroxide. , Unfortunately, it often suffers from interference. In most biological studies, the release of cytochrome c is determined by immunochemical methods. − The diagnostic utility of myoglobin immunoassay was also reported .…”

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Determination of Cytochrome c and Other Heme Proteins Using the Reduction Wave of Mercury Protoporphyrin IX Groups Generated by a Hydroxylamine Induced Replacement Reaction

Luo

Huang

2009

Anal. Chem.

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We have found that in the presence of hydroxylamine, the heme prosthetic group of the heme protein adsorbed at the mercury electrode surface reacts with mercury ion produced by the electrochemical oxidation of mercury and is quantitatively converted into the mercury protoporphyrin IX group using single-sweep polarography. As a result, the small redox peak P(0) of the heme prosthetic group at about -0.46 V (vs SCE) disappears and a large new reduction peak P of mercury protoporphyrin IX group at -0.89 V comes out in a pH 9.6 NaHCO(3)-Na(2)CO(3) solution. Peak P is extremely sensitive to heme protein concentration. On the basis of the reduction peak P, a unique electrochemical method for heme protein assays is constructed. For the cytochrome c determination, the peak height is linearly proportional to the concentration in the range of 0.005-15 mg L(-1) (correlation coefficient 0.999). The detection limit is 0.003 mg L(-1). In contrast with peak P(0), the detection limit of cytochrome c is only 0.6 mg L(-1). The voltammograms of heme proteins in the absence and presence of hydroxylamine can serve as a reliable qualitative analytical method. The chemical reaction is peculiar to the heme prosthetic group. Without hydroxylamine it cannot occur. Thereby the method is highly specific and free from interference. The performance takes only a few minutes. These advantages make the method attractive for heme protein detecting.

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Chemical analysis for small amounts of horseradish peroxidase using “porphyrinogen” as a chromogenic reagent

Cited by 5 publications

References 16 publications

β-Cyclodextrin as a Metal-anionic Porphyrin Complexation Accelerator in Aqueous Media

β-Cyclodextrin as a Metal-anionic Porphyrin Complexation Accelerator in Aqueous Media

Investigation on the effect of water on the spectroscopic behaviors of TPPS in acidic imidazolium-based ionic liquids

Determination of Cytochrome c and Other Heme Proteins Using the Reduction Wave of Mercury Protoporphyrin IX Groups Generated by a Hydroxylamine Induced Replacement Reaction

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