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PubMedDate not supplied

Luminol-hydrogen peroxide chemiluminescence produced by sweet potato peroxidase.

Anionic sweet potato peroxidase (SPP; Ipomoea batatas) was shown to efficiently catalyse luminol oxidation by hydrogen peroxide, forming a long-term chemiluminescence (CL) signal. Like other anionic plant peroxidases, SPP is able to catalyse this enzymatic reaction efficiently in the absence of any enhancer. Maximum intensity produced in SPP-catalysed oxidation of luminol was detected at pH 7.8-7.9 to be lower than that characteristic of other peroxidases (8.4-8.6). Varying the concentrations of luminol, hydrogen peroxide and Tris buffer in the reaction medium, we determined favourable conditions for SPP catalysis (100 mmol/L Tris-HCl buffer, pH 7.8, containing 5 mmol/L hydrogen peroxide and 8 mmol/L luminol). The SPP detection limit in luminol oxidation was 1.0 x 10(-14) mol/L. High sensitivity in combination with the long-term CL signal and high stability is indicative of good promise for the application of SPP in CL enzyme immunoassay.

Calibration↗

PubMed1994

Differential effects of luminol, nickel, and arsenite on the rejoining of ultraviolet light and alkylation-induced DNA breaks.

When Chinese hamster ovary cells were treated with ultraviolet (UV) light or methyl methanesulfonate (MMS), a large number of DNA strand breaks could be detected by alkaline elution. These strand breaks gradually disappeared if the treated cells were allowed to recover in a drug-free medium. The presence of nickel or arsenite during the recovery incubation retarded the disappearance of UV-induced strand breaks, whereas the disappearance of MMS-induced strand breaks was retarded by the presence of arsenite or of luminol, a new inhibitor for poly(ADP-ribose) synthetase. Luminol, however, had no apparent effect on the repair of UV-induced DNA strand breaks, and nickel had no effect on the repair of MMS-induced DNA strand breaks. When UV- or MMS-treated cells were incubated in cytosine arabinofuranoside (AraC) plus hydroxyurea (HU), a large amount of low molecular weight DNA was detected by alkaline sucrose sedimentation. The molecular weight of these DNAs increased if the cells were further incubated in a drug-free medium. This rejoining of breaks in cells pretreated with UV plus AraC and HU was inhibited by nickel and by arsenite, but not by luminol. The rejoining of breaks in cells pretreated with MMS plus AraC and HU was inhibited by luminol and by arsenite, but not by nickel. These results suggest that different enzymes may be used in DNA resynthesis and/or ligation during the repairing of UV- and MMS-induced DNA strand breaks, and that nickel, luminol, and arsenite may have differential inhibitory effects on these enzymes.

Alkylation↗

PubMed1996

Modulatory role of nitric oxide on superoxide-dependent luminol chemiluminescence.

Reactive oxygen species are involved in luminol chemiexcitation induced in biological systems, but the contribution of nitrogen-derived oxidants in the process still remains unclear. Herein, we report that luminol chemiluminescence (LCL) induced by a superoxide (O2.-)- and hydrogen peroxide (H2O2)-generating system (2-25 mU/ml xanthine oxidase plus acetaldehyde and oxygen) was markedly inhibited by nitric oxide (.NO) added either as bolus (0-10 microM) or a continuous flow (0-10 microM/min). However, the inhibition of LCL was followed by an overshoot in light emission after most .NO was consumed or the infusion stopped and was due to reactions of remaining peroxynitrite, the product of the reaction between O2.- and .NO, with luminol. Nitric oxide also inhibited peroxynitrite- and glucose oxidase-induced LCL, but no overshoot was observed. On the other hand, a continuous flux of pure peroxynitrite, at 2 to 10 microM/min, induced LCL with quantum yields close to those obtained by identical micromolar fluxes of O2.-, while peroxynitrite formed from the decomposition of the sydnonimine SIN-1 yielded 76% of the chemiluminescence obtained with authentic peroxynitrite. Peroxynitrite-induced LCL was 80 and 55% inhibitable by SOD and catalase, respectively, showing that there were O2.- and H2O2-dependent routes of chemiexcitation. The hydroxyl radical scavengers dimethyl sulfoxide, mannitol, and ethanol and the metal chelator diethylenetriaminepentaacetic acid did not inhibit peroxynitrite-induced LCL while desferrioxamine was an efficient inhibitor of light emission by reaction with an activated state of peroxynitrous acid which is responsible of performing the initial one-electron oxidation of luminol. Our results are consistent with a dual role of .NO in O2.(-)-induced LCL: (I) formation of peroxynitrite which in turn promotes the light-emitting route and (II) reaction with luminol radical intermediates directing the system toward a dark pathway. These considerations are of critical importance when analyzing cell- and tissue-derived LCL in .NO-, O2.(-)-, and peroxynitrite-producing systems.

Acridines↗

PubMed1986

Variables in xanthine oxidase-initiated luminol chemiluminescence: implications for chemiluminescence measurements in biological systems.

We tested the effects of generally used chemiluminescence inhibitors on an example of luminol chemiluminescence elicited by xanthine oxidase/hypoxanthine system, and attempted to assess their capabilities in discovering the reaction pathways leading to chemiluminescence. Luminol itself is a xanthine oxidase inhibitor and its concentration affects the reaction mechanism. Maximal chemiluminescence response was observed at luminol concentration inhibiting urate production. Chemiluminescence was totally inhibited by superoxide dismutase, the inhibition by catalase depended on luminol concentration. Ferricytochrome c, a detector of superoxide, either stimulated or inhibited chemiluminescence in a concentration-dependent manner. Chemiluminescence was highly stimulated by peroxidases. A pronounced inhibition of chemiluminescence was caused by chelators; 1 mM desferal and 0.01 mM diethyldithiocarbamate. It is suggested that measurement of luminol chemiluminescence is not a suitable method for discrimination among individual reactive oxygen species and their quantitative determination in biological systems.

Catalase↗

PubMed1996

Application of xanthine oxidase-catalyzed luminol chemiluminescence in a mouse interleukin-5 immunoassay.

A chemiluminescent substrate reagent for use in a sandwich immunoassay for the model antigen mouse interleukin-5 (IL-5) was developed using xanthine oxidase and luminol. Various parameters involved in this chemiluminescent reaction have been studied, including the substrate hypoxanthine, luminol and the Fe(II)-EDTA complex. Addition of the Fe(II)-EDTA complex enhances the chemiluminescence signal considerably. The xanthine oxidase-catalyzed chemiluminescent immunoassay was compared to horseradish peroxidase-linked immunoassays with luminol as chemiluminescent, and tetramethyl benzidine as colorimetric substrate. The detection limit of the xanthine oxidase-luminol assay was found to be about 0.6 pg/ml IL-5, whereas the peroxidase-catalyzed immunoassays have detection limits of about 1.3 (HRP-TMB) and 2.9 pg/ml (HRP-luminol) IL-5.

Animals↗

PubMed1980

Luminol-induced neutrophil chemiluminescence.

Out studies suggest that luminol directly enhances the chemiluminescence of human neutrophils. We show that a significant peak in chemiluminescence production in a particle-free system occurs between 5 and 15 min following exposure of cells to micromolar concentrations of luminol. The response is directly related to dose over a wide rane of luminol concentrations and can be inhibited by superoxide dismutase (90%), catalase (100%) and sodium azide (40%). Evidence is presented which suggests that the effect of luminol eliciting a peak in neutrophil chemiluminescence is mediated within intact cells rather than at the cell membrane. Luminol may produce a peak in chemiluminescence by stimulating very low levels of hexose monophosphate shunt activity and superoxide generation or it may simply amplify light production generated by the production of excited oxygen radicals resulting from surface interactions.

Azides↗

PubMed1986

Aqualuminescence of alkaline luminol in the presence of fluorescein.

The light yield from both luminol and fluorescein is studied at a fixed concentration of luminol and by varying the concentration of fluorescein in 3 X 10(-2) M basic solution by direct chemical reaction as well as by aqualuminescence technique. The emission spectra of chemiluminescence and aqualuminescence of the alkaline luminol-fluorescein mixture are recorded on a Fuoss spectrograph. A 4-fold increase in the aqualuminescence intensity of luminol has been observed in the presence of fluorescein as compared to that of pure luminol. The results are explained on the basis of reactions of colour centres with the activators.

Fluorescein↗

PubMed1989

What do we measure by a luminol-dependent chemiluminescence of phagocytes?

The review presents a survey of published findings concerning the mechanism of luminol-dependent chemiluminescence in biological systems. The potential of various oxygen species (superoxide anion, hydrogen peroxide, hydroxyl radical) to react with luminol is discussed. The ability of commonly used enzymes (superoxide dismutase, catalase), inhibitors, and oxygen radical scavengers to discriminate between individual oxygen species is assessed together with the potential of a variety of substances encountered in biological systems to interfere in luminol-dependent chemiluminescence reactions. It is concluded that luminol-dependent chemiluminescence gives at present very little ability to discriminate between individual oxygen or radical species. Furthermore, luminol-dependent chemiluminescence used in biological systems is extremely prone to many interferences, which are very difficult to control.

Animals↗

PubMed2003

Flow injection determination of isoniazid using N-bromosuccinimide- and N-chlorosuccinimide-luminol chemiluminescence systems.

A chemiluminescent method for the determination of isoniazid is described. 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 the isoniazid 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 isoniazid is proposed in this paper. The detection limits were 4 and 3 ng ml(-1) isoniazid for the NBS- and NCS-luminol CL systems, respectively. The relative CL intensity was linear with the isoniazid concentration in the range of 8-600 and 600-5000 ng ml(-1) for the NBS-luminol CL system, and 6-200 and 200-2000 ng ml(-1) 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↗

PubMed2002

Carbon dioxide effects on luminol and 1,10-phenanthroline chemiluminescence.

Luminol and 1,10-phenanthroline are widely used chemiluminescent (CL) reagents for the analysis of a wide range of metals and inorganic and organic complexes. While the fundamental mechanism for luminol and 1,10-phenantholine chemiluminescence is understood, the analytical application of these reagents is largely empirical and often poorly described mechanistically. For example, CL signals observed from metal-luminol systems are strongly dependent on the pH of the sample, even though the final pH of the reaction mixture is controlled to a narrow range by a buffer. Other investigators report significant changes in CL signal due to freshness and the acidity of reagents. Our work shows that many of these effects are due to dissolved CO2 present or formed in the analytical system. The hypothesis that carbon dioxide plays a pivotal role in enhancing luminol CL is supported by direct manipulation of CO2(aq) concentrations by the addition of CO2(g) or carbonic anhydrase. In contrast, Cu(II) analysis using the CL reagent 1,10-phenanthroline is completely quenched in the presence of CO2(aq). A plausible mechanism for these observations involves the reaction between superoxide, produced in these analytical systems, and CO2(aq) to form the peroxycarbonate radical, *C04-. The formation of *CO4- has very important analytical implications since this species appears to enhance or quench the CL signal from luminol and 1,10-phenanthroline, respectively.

Carbon Dioxide↗

PubMed1999

Differences in the reactivity of phthalic hydrazide and luminol with hydroxyl radicals.

The reactivity of 5-amino-2,3-dihydro-phthalazine-1,4-dione (luminol) and phthalic hydrazide with hydroxyl radicals was studied. HO*-radicals were generated by the Fenton reaction as well as by water radiolysis. Both luminol and phthalic hydrazide react with hydroxyl radicals under intense chemiluminescence (CL) emission. However, exclusively the CL arising from phthalic hydrazide oxidation can be quenched by competition (e.g. by the addition of carbohydrates), whereas luminol CL is enhanced. The reactivities of both compounds with HO*-radicals were further studied by time-resolved spectroscopy (pulse radiolysis), competition methods, NMR spectroscopy and mass spectrometry. Whereas only slight differences were detectable by pulse radiolysis, the analysis of competition kinetics in the presence of p-nitroso-dimethylaniline (NDMA) gave a two-fold-enhanced reactivity for luminol (4.8 x 10(9) l mol(-1) s(-1)) in comparison to phthalic hydrazide (2.0 x 10(9) l mol(-1) s(-1)). NMR and mass spectrometric analyses revealed significant differences in the reactivity of HO*-radicals: whereas in luminol solutions hydroxylation of the aromatic ring system predominated, hydroxylated products were not detectable upon irradiation of phthalic hydrazide. A hypothetical mechanism is proposed which may explain the observed differences.

Binding, Competitive↗

PubMedDate not supplied

Reactive oxygen species generation in human sperm: luminol and lucigenin chemiluminescence probes.

The objective of this study was to compare measurements of reactive oxygen species (ROS) generation from human spermatozoa in vitro using the luminol and lucigenin chemiluminescent probes. Luminol reacts with a variety of reactive oxygen species (H2O2, O2-, OH) and allows both intra- and extracellular ROS to be measured. Lucigenin, however, yields a chemiluminescence that is more specific for superoxide anions released extracellularly. Therefore, measurements made with both probes on the same samples should allow the intra- and extracellular components of ROS generation to be identified. Sperm samples from 47 men were divided into two equal aliquots, then processed by centrifugation and swim-up. Following further division into aliquots and the addition of the two chemiluminescent probes, Phorbol 12-myristate 13-acetate was added to trigger ROS release. Forty three percent of the sperm samples generated detectable levels of ROS. In the centrifuged preparations luminol produced a significantly higher peak luminescence than lucigenin. However, the sperm prepared by swim-up showed no significant differences in peak luminescence between luminol and lucigenin. The higher level of ROS generation produced by centrifugation may be due to membrane disruption or possibly the use of unfractionated cell suspensions. Extracellular ROS generation is more clinically important because surrounding healthy spermatozoa may be damaged. Therefore the lucigenin probe may be a more useful diagnostic tool than luminol for identifying sperm at risk of peroxidative damage after swim up preparation. The patients identified in this way may benefit from the addition of ROS scavengers to the culture medium in order to protect healthy sperm from collateral damage.

Acridines↗

PubMed1989

Spontaneous and luminol-dependent chemiluminescences from tissue preparations of benzo[a]pyrene-injected mice.

Chemiluminescence (CL) from tissue preparations of mice i.p. injected with and without the chemical carcinogen benzo[a]pyrene (BP) was detected by a single photon counting apparatus. The spontaneously emitted CL (spontaneous CL) and the CL after luminol addition (luminol-CL) were measured for mice with and without previous induction of their liver mixed-function oxidases (MFO) by phenobarbital. In MFO-non-induced mice, although the spontaneous CL was not notably modified by BP injection, the kidneys presented three times greater luminol-CL after BP injection. On the other hand, MFO-induced mice had higher spontaneous CL of plasma, liver, kidneys, and lungs, as well as higher luminol-CL of liver after BP injection, when compared with the respective MFO-induced but BP-non-injected mice. The luminol-CL of liver was suppressed by scavengers of active oxygen and free-radicals such as TIRON, butylhydroxytoluene and in a less extent by superoxide dismutase. The CL detected from tissue preparations of mice after BP treatment is thought to reflect the formation of oxygen radicals and electronically excited-species during BP metabolism.

1,2-Dihydroxybenzene-3,5-Disulfonic Acid Disodium ↗

PubMedDate not supplied

Blood transfusions impair anastomotic wound healing, reduce luminol-dependent chemiluminescence, and increase interleukin-8.

BACKGROUND/AIMS: Several studies have shown that perioperative blood transfusion increases the risk of infectious complications after surgery or trauma, however, the mechanisms behind the susceptibility to infection and impaired wound healing are not clear. This study was designed to investigate the effects of blood transfusion on anastomotic wound healing, luminol-dependent chemiluminescence, and interleukin-8. METHODOLOGY: Male Wistar rats were divided into seven groups: groups C and Tx underwent laparotomy and the other groups underwent gastrectomy and gastroduodenostomy. Groups C and G received saline; groups Tx and GT received whole blood; and groups GPT, GAT, and GRT received plasma, autologous blood, and irradiated, leukocyte-depleted whole blood, respectively. The breaking strength of the anastomosis, and plasma factor XIII, interleukin-8, and luminol-dependent chemiluminescence levels were measured. RESULTS: The plasma XIII level in group GT was significantly (P < 0.05) lower that in groups G, GPT, GAT, and GRT. The maximum breaking strength was significantly reduced in groups GT, GRT, GPT, and GAT compared to the other groups, and there was no significance between different types of transfusion. Luminol-dependent chemiluminescence levels in groups GT were severely reduced, while the and luminol-dependent chemiluminescence levels in groups GRT, GPT, and GAT were almost the same as the levels in group G. The plasma interleukin-8 levels were higher in the transfused groups, and lower in groups GRT, GPT, and GAT. CONCLUSIONS: Blood transfusions increased the incidence of anastomotic abscess and impaired anastomotic wound healing. These might be related to the reduced luminol-dependent chemiluminescence and increased interleukin-8. Autologous blood, plasma, and irradiated, leukocyte-depleted packed cells can abrogate these effects.

Anastomosis, Surgical↗

PubMedDate not supplied

[Kinetic characteristics of luminol chemiluminescence caused by chloramine compounds].

The decaying part of the kinetic curves of luminol chemiluminescence (0.02 mM) induced by N-chlorphenylalanine is approximated by an exponential dependence, which varies insignificantly as chloramine concentration is changed from 0.2 to 0.7 mM. On the whole, the chemiluminescence of luminol is a result of its oxidation, which occurs in three stages with the formation of two intermediate products. N-Chlorphenylalanine is involved in the process at the initial stage. The reciprocal of the time the luminescence reaches a maximum increases linearly with the growth of N-chlorphenylalanine concentration. According to the calculations using the equations that reflect three stages of luminol conversion in the presence of excess chloramine, the rate constant for the initial stage is about 10(3) l/(mol.min). The rate constant for one stage of the conversion of luminol oxidation product is approximately 0.2 min-1, and the rate constant of the other is severalfold greater. Luminol chemiluminescence induced by low concentrations of N,N-dichlortaurine is more durable. Probably, it is composed of two types of emission one of which slowly decays.

Alanine↗

PubMed1992

[The effect of monoclonal and polyclonal antibodies to peroxidase on combined peroxidase oxidation of 4-iodophenol with luminol and 4-aminoantipyrine].

The kinetics of peroxidase-dependent cooxidation for two substrate pairs [p-iodophenol + 4-aminoantipyrine (AAP) and p-iodophenol + luminol was studied both in the absence and presence of polyclonal antibodies (polyAB), three types of peroxidase-specific monoclonal antibodies (monoAB) and their double or triple mixtures in a wide range of H2O2 concentrations (0.01-10.0 mM). MonoAB 2C, 3E and 9D at concentrations of 0.05-500 nM inhibited the cooxidation of p-iodophenol + AAP at H2O2 concentration above 1.0 mM but activated the cooxidation of p-iodophenol + luminol. The double and triple mixtures of monoAB activated the cooxidation of p-iodophenol + AAP at the same H2O2 concentrations without any effect on the p-iodophenol + luminol cooxidation. PolyAB activated the cooxidation of p-iodophenol + AAP more effectively and only slightly activated (or inhibited) that of p-iodophenol + luminol. PolyAB diminished the values of rate constants for the interaction of the peroxidase active intermediates, E1 and E2, with p-iodophenol, AAP or luminol. Possible modes of monoAB and polyAB effects on the two substrate pair cooxidation are discussed.

Ampyrone↗

PubMed2004

Multichannel electrochemiluminescence of luminol in neutral and alkaline aqueous solutions on a gold nanoparticle self-assembled electrode.

The electrochemiluminescence (ECL) behavior of luminol on a gold nanoparticle self-assembled electrode in neutral and alkaline pH conditions was studied under conventional cyclic voltammetry (CV). The gold nanoparticle self-assembled electrode exhibited excellent electrocatalytic property and redox reactivity to the luminol ECL system. In neutral solution, four ECL peaks were observed at 0.69, 1.03, -0.45, and -1.22 V (vs SCE) on the curve of ECL intensity versus potential. Compared with a bulk gold electrode, two anodic and one cathodic ECL peaks were greatly enhanced, and one new cathodic ECL peak appeared. In alkaline solution, two anodic ECL peaks were obtained at 0.69 and 1.03 V, which were much stronger than those on a bulk gold electrode. These ECL peaks were found to depend on gold nanoparticles on the surface of the electrode, potential scan direction and range, the presence of O(2) or N(2), the pH and concentration of luminol solution, NaBr concentration, and scan rate. The emitter of all ECL peaks was identified as 3-aminophthalate by analyzing the ECL spectra. The spatial distribution of the luminol ECL peaks on the gold nanoparticle self-assembled electrode was studied by CCD. The surface state of the gold nanoparticle self-assembled electrode was characterized by scanning electron microscopy (SEM) and UV-visible reflection spectra. The mechanism for the formation of these ECL peaks has been proposed. The results indicate that the gold nanoparticle self-assembled electrode could lead to novel ECL properties, and strong luminol ECL in neutral and alkaline solutions could be obtained on such an electrode, which is of great analytical potential.

Journal Article↗

PubMedDate not supplied

Enhancer effect of fluorescein on the luminol-H2O2-horseradish peroxidase chemiluminescence: energy transfer process.

The chemiluminescence of the luminol-H2O2-horseradish peroxidase system is increased by fluorescein. Fluorescein produces an enhancement of the luminol chemiluminescence similar to that of phenolphthalein, by an energy transfer process from luminol to fluorescein. The maximum intensity and the total chemiluminescence emission (between 380 and 580 nm) of luminol with fluorescein was more than three times greater than without fluorescein; however, the emission duration was shorter. The emission spectra in the presence of fluorescein had two maxima (425 and 535 nm) and the enhancement was dependent on pH and fluorescein concentration. A mechanism is proposed to explain these effects.

Energy Transfer↗