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PubMedDate not supplied

Development of novel high-sensitivity chemiluminescence assay for luminol using thiourea derivatives.

We have screened about 100 thiourea derivatives in order to develop a sensitive chemiluminescence detection for luminol derivatives. Among these derivatives, we found a new compound, 2-(3-methylthioureido) thiazole, that could be used to measure luminol in the presence of hydrogen peroxide (H(2)O(2)). The detection limits of luminol and N-(4-aminobutyl)-N-ethylisoluminol (ABEI) were 10 fmol and 100 fmol, respectively. The mechanism of proposed chemiluminescence reaction was studied by electron spin resonance (ESR) with and without superoxide dismutase (SOD) and the addition of ethanol. The results showed that 2-(3-methylthioureido) thiazole has the ability to generate hydroxyl radical from H(2)O(2), and produces intense chemiluminescence in the presence of luminol. The proposed novel chemiluminescence reaction for luminol and luminol derivatives was applied to a high performance liquid chromatography (HPLC) assay for amino compounds.

Amino Acids↗
PubMedDate not supplied

Effect of sulphite on the oxidative metabolism of human neutrophils: studies with lucigenin- and luminol-dependent chemiluminescence.

To assess the effect of sulphite on the oxidative metabolism of human neutrophils, chemiluminescence (CL) measurements were performed using lucigenin and luminol as chemiluminigenic probes. Lucigenin-dependent CL was used for measuring superoxide anion (O2-) production, and luminol-dependent CL was used for determination of myeloperoxidase (MPO)-connected processes. With sulphite concentrations of 0.01 to 1 mmol/L, resting neutrophils showed an up to sixfold increase of lucigenin-dependent CL, but only a 1.9-fold increase of luminol-dependent CL. Subsequent stimulation of sulphite-treated neutrophils with phorbol myristate acetate (PMA) (soluble stimulant) or zymosan (particulate stimulant) resulted in an additional significant increase of lucigenin-dependent CL compared to stimulated control cells, whereas luminol-dependent CL increased slightly by 0.01 mmol/L sulphite and decreased then continuously. Sulphite concentrations above 1 mmol/L decreased both lucigenin- and luminol-dependent CL of resting and PMA- or zymosan-stimulated neutrophils. Lucigenin-dependent CL of sulphite-treated and subsequently stimulated neutrophils was strongly inhibited by extracellularly added superoxide dismutase, whereas luminol-dependent CL was markedly reduced by the MPO inhibitor azide. The intracellular activity of MPO in neutrophils stimulated with PMA in the presence of sulphite (2 mmol/L) was reduced by 55%. Sulphite (0.1 mmol/L) also inhibited strongly the activity of MPO in a cell-free system. These results indicate that micromolar concentrations of sulphite exert a stimulating effect on the O2- production of neutrophils extracellularly, but have an inhibitory effect on MPO-catalysed reactions intracellularly.

Acridines↗
PubMedDate not supplied

Luminol-, isoluminol- and lucigenin-enhanced chemiluminescence of rat blood phagocytes stimulated with different activators.

Luminol-, isoluminol- or lucigenin-enhanced chemiluminescence (CL) was used to measure the production of reactive oxygen species by rat blood leukocytes. Opsonized zymosan (OZ), phorbol-12-myristate-13-acetate (PMA), calcium ionophore A23187 (Ca-I) or N-formyl-Met-Leu-Phe (fMLP) were used as activators. The CL signal of isolated blood leukocytes decreased in rank order of luminol > isoluminol > lucigenin. The kinetic profiles of luminol- and isoluminol-enhanced CL were similar upon stimulation by each activator tested. The remarkably higher luminol and isoluminol CL responses were obtained after OZ stimulation when compared with other activators. However, when lucigenin was used, the PMA- and OZ-stimulated CL were comparable. The presence of plasma increased OZ-activated CL because of the enhanced phagocytosis of OZ. This was demonstrated by determining the phagocytosis of the fluorescent OZ using a flow cytometer. In contrast, the presence of plasma decreased PMA-activated CL, due to the antioxidant properties of plasma as determined by the CL method. As far as whole blood is concerned, only OZ activated luminol-enhanced CL was reliable. Blood volumes over 5 microL decreased CL activity due to the scavenging ability of erythrocytes. The results suggest that 0.5 microL whole blood is sufficient for routine luminol-enhanced CL analysis of whole blood oxidative burst in rats.

Acridines↗
PubMed1990

Bimodal induction of sister-chromatid exchanges by luminol, an inhibitor of poly(ADP-ribose) synthetase, during the S-phase of the cell cycle.

The cell cycle dependence of sister chromatid exchanges (SCEs) induced by luminol, a new potent inhibitor of poly(ADP-ribose) synthetase, was studied in Chinese hamster V79 cells. Continuous treatment with luminol during two whole cell cycles in the presence of 5-bromo-2'-deoxyuridine (BrdUrd), or in the first or second cycle induced SCEs very efficiently in a linear dose-dependent manner. However, no enhancement of SCE levels was observed after luminol treatment in a cycle preceding BrdUrd treatment, in contrast to results found with other strong SCE inducers such as cis-diammine-dichloroplatinum (II) (CDDP) and mitomycin C (MMC). Luminol was about ten times as effective in inducing SCEs as 3-aminobenzamide (3AB)', an inhibitor of the NAD+ site of poly(ADP-ribose) synthetase. The induction of SCEs by luminol was restricted to the S-phase of the cell cycle with peaks at an early and a late stage, corresponding to the biphasic replication of DNA. The mechanism of SCE appears to be the same at the early and late stages of S-phase for luminol-induced SCE formation.

Animals↗
PubMed1993

Luminol and diazoluminomelanin as indicators of HL-60 cell differentiation.

This paper describes use of a novel substituted melanin which is useful in detection of differentiating leukemia cells and their membranes. Comparisons of luminol-(5-amino-2,3-dihydro-1,4-phthalazinedione) and diazoluminomelanin (DALM)-mediated chemiluminescence (CL) were made with various types of differentiated and undifferentiated HL-60 whole cells, cell lysates, and membrane fractions. Luminol had a greater CL response than DALM with HL-60 promyelocytic stem cells and differentiated macrophage-like or neutrophil-like whole cell and cell lysate preparations. However, DALM showed markedly greater CL than luminol for membrane fractions derived from each cell type. The greatest luminol-dependent CL was observed for cell types high in myeloperoxidase (MPO). The greatest DALM-mediated CL was seen with cell types that are high in MPO or strong producers of superoxide (O2-) anions. In some cases, significant differences in CL could also be distinguished on the basis of inducing agent used [i.e. dimethylsulfoxide, all-trans retinoic acid or 12-o-tetradecanoylphorbol-13-acetate]. Both luminol- and DALM-dependent CL were strongly inhibited by preincubation of cellular preparations with 3-amino-L-tyrosine (a component of DALM). Taken together, these data suggest that the reaction mechanism of luminol favors interaction with cytoplasmic MPO whereas that of DALM favors membrane interactions. Thus, both reagents may be of use in assays to detect differentiating leukocytes or their cellular components.

Adult↗
PubMed2004

Flow-injection determination of isoniazid using sodium dichloroisocyanurate- and trichloroisocyanuric acid-luminol chemiluminescence systems.

A chemiluminescent (CL) method for the determination of isoniazid is described. The method is based on the CL generated during the oxidation of luminol by sodium dichloroisocyanurate (SDCC) and trichloroisocyanuric acid (TCCA) in alkaline medium. It was found that isoniazid greatly enhances this CL intensity when present in the luminol solution. Based on this observation, a new flow-injection CL method for the determination of isoniazid has been proposed in this paper. The detection limits were 2 and 3 ng ml(-1) isoniazid for the SDCC-luminol and TCCA-luminol CL systems, respectively. The relative CL intensity was linear with the isoniazid concentration in the range of 4-100 and 100-200 ng ml(-1) for the SDCC-luminol CL system, and 6-200 and 200-1000 ng ml(-1) for the TCCA-luminol CL system. The results obtained for the assay of pharmaceutical preparations compared well with those obtained by the official methods and demonstrated good accuracy and precision.

Chemistry Techniques, Analytical↗
PubMed1999

Detection of mitochondria-derived reactive oxygen species production by the chemilumigenic probes lucigenin and luminol.

Both lucigenin and luminol have widely been used as chemilumigenic probes for detecting reactive oxygen species (ROS) production by various cellular systems. Our laboratory has previously demonstrated that lucigenin localizes to the mitochondria of rat alveolar macrophages and that lucigenin-derived chemiluminescence (CL) appears to reflects superoxide O2(-.) production by mitochondria in the unstimulated macrophages. In this study, we further examined the ability of lucigenin- and luminol-derived CL to assess O2(-.) and H2O2 formation, respectively, by isolated intact mitochondria. Mitochondria were isolated from monocytes/macrophages differentiated from monoblastic ML-1 cells. Incubation of the substrate-supported mitochondria with lucigenin at non-redox cycling concentration produced lucigenin-derived CL. Luminol-derived CL was also elicited with substrate-supplemented mitochondria in the presence of horseradish peroxidase (HRP). The lucigenin-derived CL was diminished extensively by the membrane permeable superoxide dismutase (SOD) mimetics, 2,2,6, 6-tetramethylpiperidine-N-oxyl and Mn(III) tetrakis(1-methyl-4-pyridyl)porphyrin, but not by Cu,Zn-SOD. On the other hand, luminol-derived CL was not observed in the absence of HRP and was significantly inhibited by catalase. A spectrum of agents known to specifically affect mitochondrial respiration exhibited corresponding effects on both lucigenin- and luminol-derived CL. Taken together, our results demonstrate that with isolated mitochondria lucigenin-derived CL monitors intramitochondrial O2(-.) production by the mitochondrial electron transport chain, whereas the luminol-derived CL detects H2O2 released from the mitochondria. As such, use of both probes provides a comprehensive and clear assessment of ROS production by mitochondria.

Acridines↗
PubMed1986

A demonstration that O2- is a crucial intermediate in the high quantum yield luminescence of luminol.

The chemiluminescence of luminol, due to its reaction with alkaline H2O2, is inhibited by superoxide dismutase or by hydroxyl radical scavengers. Hematin markedly enhances this H2O2-induced luminescence of luminol and lessens, but does not eliminate, the sensitivity towards these inhibitors. Reaction mechanisms are proposed to account for these results. Since luminol luminescence depends upon a reaction between the luminol radical and O2-, and since the luminol radical can reduce dioxygen to O2-, superoxide dismutase-inhibitable luminol luminescence cannot be reliably used as a detector of O2- production.

Hemin↗
PubMed2004

The enhanced electrochemiluminescence of luminol on the nickel phthalocyanine modified electrode.

A glassy carbon electrode (GCE) modified with nickel(II) tetrasulfophthalocyanine (NiTSPc) and Nafion was used for the investigation of the catalytic oxidation of luminol. The modified electrode was found to much more effectively improve the emission of electrochemiluminescence(ECL) of luminol in a solution containing hydrogen peroxide. The enhanced ECL signal corresponded to the catalytic oxidation of both luminol and H(2)O(2) by NiTSPc. Attached Ni(II) on GCE was oxidised to Ni(III) and then used as the catalyst for the chemiluminescence of luminol. The enhanced stability of the ECL signal with Nafion would mainly result from the prevention of the dissolution of NiTSPc and the adsorption of the oxidation product of luminol on the electrode surface. The proposed method enables a detection limit for luminal of 6.0 x 10(-8) mol L(-1) to be achieved in the presence of H(2)O(2) in the neutral solution. The enhanced ECL intensity had a linear relationship with the concentration of luminol in the range of 1.0 x 10(-7)-8.0 x 10(-6) mol L(-1).

Carbon↗
PubMed1999

The effect of luminol on presumptive tests and DNA analysis using the polymerase chain reaction.

This study was designed to test the following factors involved with processing luminol treated bloodstained evidence: 1) The reactivity of other presumptive chemical color tests, phenolphthalin (PT) and tetramethylbenzidine (TMB), following the application of the light emitting luminol presumptive test. 2) The effect of different cleanings of various bloody substrates on the luminol test. 3) The effect of different cleanings of various bloody substrates on the ability to obtain DNA suitable for PCR testing. 4) The ability to extract DNA from luminol treated bloodstained substrates using three extraction techniques. 5) The effect of spraying washed and unwashed bloodstains on various substrates with luminol on the ability to correctly type the DNA using PCR. Our findings indicated that luminol did not adversely effect the PCR testing and did not interfere with the PT and TMB presumptive tests for blood. It was determined that the substrate and the method of cleaning were the major factors affecting DNA yield and the ability to type the bloodstains using PCR based technologies.

Benzidines↗
PubMed1983

Role of myeloperoxidase in the luminol-dependent chemiluminescence response of phagocytosing human monocytes.

The luminol-dependent chemiluminescence (CL)-response of phagocytosing declined steadily during in vitro differentiation and was approximately 10% of the initial value by the fourth day of culture. A parallel decline in myeloperoxidase (MPO)-activity of monocyte cell lysates was observed during the same period, and a close correlation was found between peak luminol-dependent CL-response and MPO-activity. The lucigenin-dependent CL-response of phagocytosing monocytes in parallel cultures declined to about 85% of the initial value during four days of in vitro culture. Chemiluminescence was determined in solutions of luminol or lucigenin subjected to fixed amounts of H2O2 or enzymatically generated fluxes of H2O2. Horseradish peroxidase (HRPO) markedly enhanced the luminol-dependent CL but not the lucigenin-dependent CL of this cell-free system. Similar results were obtained when a crude MPO extract was substituted for the HRPO. Despite this evidence that luminol-dependent CL is enhanced by peroxidases, addition of HRPO to the assay medium did not increase the luminol-dependent CL-response of four days old, phagocytosing monocytes.

Acridines↗
PubMed2007

Comparative studies on electrogenerated chemiluminescence of luminol on gold nanoparticle modified electrodes.

Comparative studies on the electrogenerated chemiluminescence (ECL) behavior of luminol on various electrodes modified with gold nanoparticles of different size were carried out in neutral solution by conventional cyclic voltammetry (CV). The results demonstrated that the gold nanoparticle modified electrodes could generate strong luminol ECL in neutral pH conditions. The catalytic performance of gold nanoparticle modified electrodes on luminol ECL depended not only on the gold nanoparticles but also on the substrate. Gold electrode and glassy carbon electrode were the most suitable substrates for the self-assembly of gold nanoparticles. Moreover, the gold nanoparticle modified gold and glassy carbon electrode had satisfying stability and reproducibility and did not need tedious pretreatment of electrode surface before each measurement. It was also found that luminol ECL behavior depended on the size of gold nanoparticles. The most intense ECL signals were obtained on a 16-nm-diameter gold nanoparticle modified electrode. The modified electrode prepared by the self-assembly method exhibited much better catalytic effect on luminol ECL than that prepared by the electrically deposited method. The ECL behavior of luminol on a gold nanoparticle self-assembled gold electrode was also investigated by other transient-state electrochemical techniques, such as chronoamperometry, differential pulse voltammetry, normal pulse voltammetry, and square wave voltammetry. The strongest ECL intensity was obtained under square wave voltammetric condition.

Journal Article↗
PubMedDate not supplied

A new screening method to detect water-soluble antioxidants: acetaminophen (Tylenol) and other phenols react as antioxidants and destroy peroxynitrite-based luminol-dependent chemiluminescence.

This study is based on a simple chemical interaction of peroxynitrite (O = N-O-O-) and luminol, which produces blue light upon oxidation. Since peroxynitrite has a half-life of about 1 s, a drug known as linsidomine (SIN-1) is used as a peroxynitrite generator. Peroxynitrite can oxidize lipids, proteins and nucleic acids. Upon the stimulation of inflammation and/or infection, macrophages and neutrophils can be induced to produce large amounts of peroxynitrite, which can oxidize phenols and sulphhydryl-containing compounds. Therefore, phenols and sulphhydryls eliminate peroxynitrite. This is an example of the Yin-Yang hypothesis e.g. oxidation-reduction. Acetaminophen (Tylenol) can inhibit fever and some types of pain without being a particularly effective anti-inflammatory. Since it is a phenol, it could act as a nitration target for peroxynitrite. Then peroxynitrite, the possible cause of pain and elevated temperature, might be destroyed in the reaction. Acetaminophen is a phenolic compound which produces a clear inhibitory dose-response curve with peroxynitrite in its range of clinical effectiveness. Whether acetaminophen actually works as we suggest is to be proven. Three different types of reaction could decrease the amount of peroxynitrite: (a) interference with base-catalysed opening of the SIN-1 molecule; (b) destruction of one or both substances needed to form it--superoxide and/or nitric oxide; when the SIN-1 degrades to superoxide and nitric oxide, the former may be destroyed by superoxide dismutase (SOD); (c) peroxynitrite may react directly with phenols (mono-, di-, tri- and tetraphenols), possibly by nitration. Nordihydroguaiaretic acid and 2-hydroxyestradiol (catechol estrogen) are potent inhibitors of luminol light emission. Epineprine, isoproterenol, pyrogallol, catechol and ascorbic acid (a classic antioxidant) are all inhibitors of luminol chemiluminescence. Isoproterenol, norepinephrine/and epinephrine first inhibit light but overall stimulate the light production. Initially, SIN-1 degrades to produce peroxynitrite, which reacts with luminol to produce blue light. If any of three catecholamines are present with the reaction that produces light, there is an initial inhibition of light production, and then a marked stimulation. A possible reason for this is that these catechols are oxidized and the metabolized phenol stimulates the production of light from luminol. Also, during oxidation of catecholamines superoxide is sometimes formed, which could stimulate production of peroxynitrite. This simple screening system is introduced to find useful antioxidants against peroxynitrite.

Acetaminophen↗
PubMedDate not supplied

Comparative studies of the chemiluminescent horseradish peroxidase-catalysed peroxidation of acridan (GZ-11) and luminol reactions: effect of pH and scavengers of reactive oxygen species on the light intensity of these systems.

In this study, the chemiluminescent horseradish peroxidase/H(2)O(2)-catalysed oxidation of acridan (GZ-11) substrate was compared with the well-characterized light-producing luminol reaction. p-Iodophenol and p-phenylphenol were used as enhancers, respectively, for the luminol and acridan reactions. These two light-producing systems showed significant differences in relation to the effect of pH, as well as the effect of scavengers of reactive oxygen species, on the light intensity. Light production measured could be as low as pH 2.6 in the acridan reaction, whereas light emission was not detected in the luminol system below pH 5.6. In contrast with the luminol system, it was found that superoxide dismutase does not inhibit the light intensity of the acridan system. This suggests that superoxide anion does not participate in the mechanism of the light-emitting steps of the acridan reaction. Addition of hydroxyl radical scavengers, mannitol and benzoate, to the acridan reaction medium had no appreciable effect on the chemiluminescent intensity, indicating that hydroxyl radicals do not interfere in light-emitting steps. In addition, the peroxidation of the acridan substrate was found to be very slow at pH 5.6 in the absence of the enhancer, p-phenylphenol, whereas in its presence a rapid degradation of the acridan substrate was observed. Therefore, it is suggested that the enhancer might be initially oxidized by the HRP/H(2)O(2) system, resulting in the formation of the enhancer radical, which could be the actual oxidizing agent of the acridan substrate. Together, the data presented in this paper indicate that the chemiluminescent horseradish peroxidase-catalysed peroxidation of acridan (GZ-11) is more specific than the luminol reaction for the reactive oxygen species involved in the light-emitting steps, i. e, H(2)O(2).

Acridines↗
PubMedDate not supplied

Enhancement and inhibition of luminol chemiluminescence by phenolic acids.

We explored the behaviour of a series of phenolic acids used as enhancers or inhibitors of luminol chemiluminescence by three different methods to determine if behaviour was associated with phenolic acid structure and redox character. All the phenolic acids inhibited chemiluminescence when hexacyanoferrate (III) was reacted with the phenolic acids before adding luminol. The redox character of these compounds was clearly related to structure. When hexacyanoferrate(III)-luminol-O2 chemiluminescence was initiated by phenolic acid-luminol mixtures some phenolic acids behaved as enhancers of chemiluminescence, and others as inhibitors. We propose a mechanism to explain these findings. We found direct relationships between the redox character of the phenolic acids and the enhancement or inhibition of the chemiluminescence of the luminol-H2O2-peroxidase system and we propose mechanism to explain these phenomena.

Cinnamates↗
PubMedDate not supplied

Optimization of peroxynitrite-luminol chemiluminescence system for detecting peroxynitrite in cell culture solution exposed to carbon disulphide.

We established a peroxynitrite-luminol chemiluminescence system for detecting peroxynitrite in cell culture solution exposed to carbon disulphide (CS(2)). Three factors, including exposure time to ozone (Factor A), volume of peroxynitrite (ONOO(-)) solution (Factor B) and luminol concentrations (Factor C) at three levels were selected and the combinations were in accordance with orthogonal design L(9) (3(4)). Peroxynitrite was generated from the reaction of ozone and 0.01 mol/L sodium azide (NaN(3)) dissolved in carbonic acid buffer solution (pH 11), and it was reacted with luminol to yield chemiluminescence. The peak value, peak time and kinetic curve of the light emission were observed. The selected combination conditions were 50 s ozone, 800 micro L peroxynitrite and 0.001 mol/L luminol solution. Cell culture solution with CS(2) enhanced the emission intensity of chemiluminescence (F = 8.38, p = 0.018) and shortened the peak time to chemiluminescence (F = 139.00, p = 0.0001). The data demonstrated that this luminol chemiluminescence system is suitable for detecting peroxynitrite in cell culture solutions for evaluating the effect of CS(2) on endothelial cells.

Carbon Disulfide↗
PubMedDate not supplied

Flow injection analysis of riboflavin with chemiluminescence detection using a N-halo compounds-luminol system.

A chemiluminescent method for the determination of riboflavin is described. The method is based on the chemiluminescence (CL) generated during the oxidation of luminol by N-bromosuccinimide (NBS) and N-chlorosuccinimide (NCS) in alkaline medium. It was found that riboflavin could greatly enhance this CL intensity when present in the luminol solution. Based on this observation, a new flow-injection CL method for the determination of riboflavin is proposed in this paper. The detection limits were 7.5 ng/mL and 3.5 ng/mL of riboflavin for the NBS- and NCS-luminol CL systems, respectively. The relative CL intensity was linear, with riboflavin concentration in the range 19-600 ng/mL and 600-2000 ng/mL for the NBS-luminol CL system, and 12-200 ng/mL and 200-2000 ng/mL for the NCS-luminol CL system. The results obtained for the assay of pharmaceutical preparations compared well with those obtained by the official method and demonstrated good accuracy and precision.

Bromosuccinimide↗
PubMedDate not supplied

Electrogenerated chemiluminescence of luminol in neutral and alkaline aqueous solutions on a silver nanoparticle self-assembled gold electrode.

The electrochemiluminescence (ECL) behaviour of luminol on a silver nanoparticle self-assembled gold electrode in neutral and alkaline solutions was investigated using conventional cyclic voltammetry (CV). The silver nanoparticle self-assembled gold electrode exhibited excellent ECL properties for the luminol ECL system. In neutral solutions, four ECL peaks (ECL-1-ECL-4) were observed at 0.73, 1.15, -0.46 and -1.35 V (vs. SCE), respectively. The intensities of these peaks were enhanced significantly compared with those on a bulk gold electrode and a gold nanoparticle self-assembled gold electrode. It was found that ECL-1 and ECL-2 on a silver nanoparticle-modified electrode were about 1000 and 1770 times stronger than those on a bare Au electrode and were about 17 and 15 times stronger than those on a gold nanoparticle-modified electrode, respectively. In alkaline solutions, four ECL peaks were also observed that were much stronger than those in neutral solutions, and ECL-1 and ECL-2 were enhanced by about three orders and one order of magnitude compared with those on a bare Au electrode and on a gold nanoparticle self-assembled electrode, respectively. Moreover, the silver nanoparticle-modified electrode exhibited good stability and reproducibility for luminol ECL. These peaks were found to depend on a number of factors, including silver nanoparticles on the surface of the modified electrode, potential scan direction, scan rate, scan range, the presence of O2 or N2, pH values, the concentrations of NaBr and luminol, and buffer solutions. The emitter of the ECL was confirmed as 3-aminophthalate by analysing the CL spectra. The surface state of the silver nanoparticle self-assembled electrode was characterized by scanning electron microscopy (SEM) and the interface property of the electrode was studied by electrochemical impedance spectroscopy (EIS). A mechanism for the formation of these ECL peaks is proposed. The results demonstrate that luminol has excellent ECL properties, such as strong ECL intensity and good reproducibility on a silver nanoparticle-modified gold electrode, in both neutral and alkaline solutions, which is of great potential in analytical applications.

Air↗