Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Luminol”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 19 recordsLinked to original sources
PubMed1999

Luminol activity of horseradish peroxidase mutants mimicking a proposed binding site for luminol in Arthromyces ramosus peroxidase.

To enhance the oxidation activity for luminol in horseradish peroxidase (HRP), we have prepared three HRP mutants by mimicking a possible binding site for luminol in Arthromyces ramosus peroxidase (ARP) which shows 500-fold higher oxidation activity for luminol than native HRP. Spectroscopic studies by (1)H NMR revealed that the chemical shifts of 7-propionate and 8-methyl protons of the heme in cyanide-ligated ARP were deviated upon addition of luminol (4 mM), suggesting that the charged residues, Lys49 and Glu190, which are located near the 7-propionate and 8-methyl groups of the heme, are involved in the specific binding to luminol. The positively charged Lys and negatively charged Glu were introduced into the corresponding positions of Ser35 (S35K) and Gln176 (Q176E) in HRP, respectively, to build the putative binding site for luminol. A double mutant, S35K/Q176E, in which both Ser35 and Gln176 were replaced, was also prepared. Addition of luminol to the HRP mutants induced more pronounced effects on the resonances from the heme substituents and heme environmental residues in the (1)H NMR spectra than that to the wild-type enzyme, indicating that the mutations in this study induced interactions with luminol in the vicinity of the heme. The catalytic efficiencies (V(max)/K(m)) for luminol oxidation of the S35K and S35K/Q176E mutants were 1.5- and 2-fold improved, whereas that of the Q176E mutant was slightly depressed. The increase in luminol activity of the S35K and S35K/Q176E mutants was rather small but significant, suggesting that the electrostatic interactions between the positive charge of Lys35 and the negative charge of luminol can contribute to the effective binding for the luminol oxidation. On the other hand, the negatively charged residue would not be so crucial for the luminol oxidation. The absence of drastic improvement in the luminol activity suggests that introduction of the charged residues into the heme vicinity is not enough to enhance the oxidation activity for luminol as observed for ARP.

Amino Acid Substitution↗
PubMedDate not supplied

What do we measure with luminol-, lucigenin- and penicillin-amplified chemiluminescence? 1. Investigations with hydrogen peroxide and sodium hypochlorite.

Evidence is provided that the amplifiers luminol and lucigenin react with different reactive oxygen species (ROS), depending on the ROS-generating system used. H2O2 is used to produce calibration curves for luminol- and lucigenin-amplified chemiluminescence. With this chemiluminescence generator we characterized the specificity and sensitivity of luminol- and lucigenin-amplified chemiluminescence and also studied penicillin G, a known enhancer of luminol-amplified chemiluminescence. The combination of luminol and lucigenin in reciprocally changing concentrations is effective in an additive manner, but the weak amplifier penicillin increases luminol-amplified chemiluminescence distinctly more than in an additive manner in different combinations. Lucigenin-amplified chemiluminescence is increased by penicillin at about 1% of the optimum concentration of penicillin; increasing concentrations of penicillin are less and less effective. On the other hand, low lucigenin concentrations enhance penicillin-amplified chemiluminescence at optimum penicillin concentrations more than in an additive manner. Fe2+ does not alter luminol-, lucigenin- or penicillin-amplified chemiluminescence. Co2+ increases luminol-amplified chemiluminescence by a factor of 100. Lucigenin- and penicillin-amplified chemiluminescence are minimally enhanced by Co2+. Cu2+ enhances luminol-amplified chemiluminescence with increasing concentrations by a factor of 1000. Lucigenin-amplified chemiluminescence increases also by the factor of 1000, but the concentration-reaction curve is not as steep. NaOCl enhances H2O2/Fe(2+)-driven luminol-amplified chemiluminescence in a concentration-dependent manner by a factor of 10(4) (in the highest concentration of 10 mmol/L) and lucigenin amplified chemiluminescence only by a factor of about 25. Catalase (CAT) abolishes luminol-, lucigenin- and penicillin-amplified chemiluminescence completely, whereas superoxide dismutase (SOD) has no effect on luminol- or penicillin-amplified chemiluminescence, but enhances lucigenin-amplified chemiluminescence five-fold increasingly with increasing SOD activity.

Acridines↗
PubMed1998

One- and two-electron oxidations of luminol by peroxidase systems.

The kinetics of luminol oxidation catalyzed by horseradish peroxidase (HRP), Arthromyces ramosus peroxidase (ARP) and lactoperoxidase (LPO) at pH 7.0 was investigated. One-electron oxidation of luminol by peroxidase systems was inferred from the detection of luminol radicals, luminol-mediated formation of ascorbate radicals, and the trapping of luminol-mediated GSH radicals. The catalytic intermediate of peroxidases in the steady state was Compound II and the rate constants of HRP, ARP, and LPO Compound II with luminol were 3.6 x 10(4), 1.1 x 10(7), and 2.5 x 10(4) M(-1)s(-1), respectively. The intensity of luminol chemiluminescence (CL) generated by the peroxidases depended on the rate constants of the rate-determining step. The luminol CL catalyzed by peroxidases increased with an increase in the concentration of H2O2 and was inhibited in the presence of catalase. Neither oxygen consumption during the reaction under aerobic conditions nor a change of light intensity under anaerobic conditions was observed. The light emission and oxidation of luminol catalyzed by LPO was increased by trace amounts of iodide. LPO catalyzes two-electron oxidations of iodide to form iodinating intermediate (Nakamura, M.; et al. J. Biol. Chem. 260:13546-13552, 1985), which subsequently oxidizes luminol. The results lead us to conclude that CL of luminol was initiated by peroxidase systems irrespective of one- or two-electron oxidations of luminol.

Catalase↗
PubMedDate not supplied

The phagocyte chemiluminescence paradox: luminol can act as an inhibitor of neutrophil NADPH-oxidase activity.

The chemiluminescence system amplified by luminol or isoluminol is a sensitive and widely used method for determination of respiratory burst products generated by the NADPH-oxidase in phagocytes. The present study shows that luminol, but not isoluminol, can inhibit the release of oxygen metabolites generated by human neutrophil NADPH-oxidase. The difference in structure between luminol and isoluminol (rendering luminol more lipophilic than isoluminol, and thereby membrane-permeable), is suggested to determine indirectly whether or not the molecule is inhibitory. Luminol was shown to have an increased inhibitory effect after preincubation of neutrophils on a surface of aggregated IgG, suggesting that the cells can be transferred from a 'luminol-insensitive' to a 'luminol-sensitive' state. Since luminol had no inhibitory effect in a cell-free NADPH-oxidase system, it is likely that it interferes with the signal transduction pathway, leading to assembly and/or activation of the oxidase. As a consequence of the present results, showing that luminol but not isoluminol can inhibit NADPH-oxidase activity, we suggest that isoluminol is used in future studies of superoxide anion release from phagocytes.

Cell-Free System↗
PubMed1995

Nitric oxide synthase inhibitors decrease human polymorphonuclear leukocyte luminol-dependent chemiluminescence.

Nitric oxide synthase (NOS) inhibitors have been reported to modulate luminol-dependent chemiluminescence (CL) in rat macrophages, whereas the potent oxidant peroxynitrite (ONOO-) was shown to react with luminol to yield CL in a cell-free system. We evaluated the role of the L-arginine/NOS pathway in luminol CL by phorbol ester-activated human polymorphonuclear (PMN) leukocytes using the NOS inhibitors NG-monomethyl-L-arginine (L-NMMA) and N-iminoethyl-L-ornithine (L-NIO). Nitric oxide (.NO) release was determined by oxidation of oxymyoglobin. In addition, the effect of NOS inhibitors on superoxide anion O2.-) production was measured. Luminol CL was notably diminished by L-NMMA in a dose-dependent manner. Superoxide dismutase (SOD) also decreased luminol CL and L-NMMA potentiated light emission decrease produced by SOD. Nitric oxide and O2.- production was significantly decreased by L-NMMA; moreover, luminol-dependent CL but not O2.- production was attenuated by L-NIO. These data suggest that products of catalytic activity of both .NO synthase and NADPH oxidase are required to elicit maximal luminol CL in this system. These studies demonstrate that the NOS synthase pathway is involved in luminol CL by human PMN, and they suggest that ONOO- would be an unrecognized mediator in this phenomenon.

Animals↗
PubMed1993

Peroxynitrite-induced luminol chemiluminescence.

Vascular endothelial cells, smooth muscle cells, macrophages, neutrophils, Kupffer cells and other diverse cell types generate superoxide (O2.-) and nitric oxide (.NO), which can react to form the potent oxidant peroxynitrite anion (ONOO-). Peroxynitrite reacted with luminol to yield chemiluminescence which was greatly enhanced by bicarbonate. The quantum chemiluminescence yield of the ONOO- reaction with luminol in bicarbonate was approx. 10(-3). Chemiluminescence was superoxide dismutase-inhibitable, indicating that O2.- was a key intermediate for chemiexcitation. O2.- appears to be formed secondarily to the reaction of a bicarbonate-peroxynitrite complex with luminol, yielding luminol radical and O2.-. Luminol radical reacts with O2.- to form the unstable luminol endoperoxide, which follows the light-emitting pathway. Neither .NO nor O2.- alone were capable of directly inducing significant luminol chemiluminescence in our assay systems. These results suggest that ONOO- can be a critical unrecognized mediator of cell-derived luminol chemiluminescence reported in previous studies. In addition, it is shown that bicarbonate can participate in secondary oxidation reactions after reacting with ONOO-.

Antioxidants↗
PubMedDate not supplied

Lucigenin- and luminol-enhanced chemiluminescence in turkey monocytes.

Monocytes from 10 week-old specific pathogen-free turkeys were isolated from peripheral blood by density centrifugation and assayed for their oxidative activity by means of a luminometer. Chemiluminescence (CL) properties after stimulation with different soluble and particulate stimuli were compared in lucigenin- and luminol-enhanced assays. A distinct response could be measured with 12-phorbol 13-myristate acetate (PMA) and Zymosan A, but only a weak signal was obtained with calcium ionophore A23187. No oxidative activity could be induced with N-formyl-methionyl-phenylalanine. Peak maxima for both lucigenin- and luminol-enhanced CL were ranked: PMA > Zymosan A > calcium ionophore. The velocity of the lucigenin- and luminol-enhanced responses induced by calcium ionophore were of similar magnitude, but the lucigenin-enhanced responses of Zymosan A and PMA-stimulated monocytes were respectively about 5 and 10 times higher than those obtained in luminol-enhanced assays. No peroxidase activity could be detected in the purified turkey monocytes. As luminol-enhanced CL primarily results from the peroxidase activity, this lack of myeloperoxidase may explain the observed lower responses to the different stimuli, in the presence of a luminol. In contrast, lucigenin-enhanced CL is not related to peroxidase activity, but is a selective probe of oxidase activity. Irrespective of the myeloperoxidase deficiency, different soluble and particulate stimuli induced a significant and reproducible CL response in turkey monocytes, in the presence of both chemiluminigenic probes, lucigenin and luminol. The possibility of measuring the phagocyte oxygenation activity of turkey monocytes represents a useful tool for the study of monocyte mediated host defence in the turkey.

Acridines↗
PubMed1993

Luminol chemiluminescence in rat macrophages and granulocytes: the role of NO, O2-/H2O2, and HOCl.

Luminol chemiluminescence was increased up to five-fold by L-arginine and markedly inhibited by NG-nitro-L-arginine (L-NNA) in phorbol ester (PMA) or opsonized zymosan-activated rat Kupffer cells, and in PMA-activated rat peritoneal and alveolar macrophages. While in Kupffer cells these effects did occur without pretreatment with lipopolysaccharides (LPS), LPS pretreatment was a requirement in peritoneal and alveolar macrophages. Azide (0.05 mM) had no effect on luminol chemiluminescence in the macrophages. The changes in luminol chemiluminescence were accompanied by parallel changes in nitric oxide (NO) formation. Macrophage superoxide anion radical (O2-) production was not significantly changed by addition of L-arginine and L-NNA nor by pretreatment with LPS. No hypochlorous acid (HOCl) formation was detectable in the macrophages. In contrast, in rat granulocytes activated by a variety of stimuli including PMA, zymosan, the chemotactic peptide formyl-methionyl-leucyl-phenylalanine and the calcium ionophore A23187 with or without pretreatment with LPS, L-arginine and L-NNA had no effect on luminol chemiluminescence. Luminol chemiluminescence, however, was largely inhibited by 0.05 mM azide. The activated granulocytes released significant amounts of HOCl but did not generate NO. These results demonstrate that NO may largely contribute to luminol chemiluminescence in rat macrophages, in which HOCl formation does not occur. On the other hand, HOCl is the reactive oxygen species responsible for luminol chemiluminescence in rat granulocytes, where NO is formed only in minor quantities, if at all.

Animals↗
PubMed1991

On radical production by PMA-stimulated neutrophils as monitored by luminol-amplified chemiluminescence.

The means by which neutrophils within the body ward off infectious and neoplastic processes by the activation of molecular oxygen, as well as how such mechanisms dysfunction, is the subject of extensive ongoing research. Most previous studies of neutrophil activation indicate that there is a transient production of reactive oxygen species. Luminol-amplified chemiluminescence surveillance of O2-. and H2O2 supported these general findings. Yet, recent studies showed that production of reactive oxygen species by PMA-stimulated neutrophils is not transient but persistent; however, luminol-dependent methods do not corroborate such findings. The kinetics of O2-. production by human neutrophils were studied using luminol-amplified chemiluminescence (CL), spin trapping combined with electron spin resonance detection, and ferricytochrome c reduction. The effects of pH and O2 level on luminol-amplified CL were determined using hypoxanthine/xanthine oxidase to produce O2-. and H2O2 in cell-free systems. As we have found by electron spin resonance and ferricytochrome c reduction, stimulated neutrophils continued to generate O2-. for several hours, yet when luminol-amplified CL was used to continuously follow radical production, CL was shortly lost. Similar loss of CL was observed with continuous enzymatic formation of O2-. and H2O2. The failure of the CL assay to report O2-. and H2O2 formation results from some luminol reaction product which interferes with the light reaction. Our results show that the cells are operative for long periods indicating that cell exposure to prolonged O2-. fluxes does not terminate radical production, and even when pH, [O2], and reagents are optimized, the use of luminol-amplified CL is not a valid assay for continuous monitoring of O2-. and H2O2 generated by either stimulated neutrophils or in cell-free systems.

Cell-Free System↗
PubMedDate not supplied

Phenol derivatives as enhancers and inhibitors of luminol-H2O2-horseradish peroxidase chemiluminescence.

Systematic studies on phenol derivatives facilitates an explanation of the enhancement or inhibition of the luminol-H2O2-horseradish peroxidase system chemiluminescence. Factors that govern the enhancement are the one-electron reduction potentials of the phenoxy radicals (PhO./PhOH) vs. luminol radicals (L./LH-) and the reaction rates of the phenol derivatives with the compounds of horseradish peroxidase (HRP-I and HRP-II). Only compounds with radicals with a similar or greater reduction potential than luminol at pH 8.5 (0.8V) can act as enhancers. Radicals with reduction potentials lower than luminol behave in a different way, because they destroy luminol radicals and inhibit chemiluminescence. The relations between the reduction potential, reaction rates and the Hammett constant of the substituent in a phenol suggest that 4-substituted phenols with Hammett constants (sigma) for their substituents similar or greater than 0.20 are enhancers of the luminol-H2O2-horseradish peroxidase chemiluminescence. In contrast, those phenols substituted in position 4 for substituents with Hammett constants (sigma) lower than 0.20 are inhibitors of chemiluminescence. On the basis of these studies, the structure of possible new enhancers was predicted.

Free Radicals↗
PubMedDate not supplied

Effect of antioxidants on induction time of luminol luminescence elicited by 3-morpholinosydnonimine (SIN-1).

The reaction between luminol as a chemiluminescence probe and 3-morpholinosydnonimine (SIN-1) as a peroxynitrite donor was evaluated in order to determine the action of several antioxidants. Several well-known antioxidants found in biological fluids or cells modify the light profile of the reaction between SIN-1 and luminol. One main modification was characterized by a transient suppression of the light signal, thus permitting evaluation of an induction time (sigma) which is linearly related to the concentration of the additive. From induction time measurements and using Trolox as a reference antioxidant, the trapping ability of a compound against oxidants and radicals produced in the luminol-SIN-1 reaction at pH 7. 4 was determined. Uric acid showed higher antioxidant capacity than Trolox, while bilirubin and ascorbic acid, in decreasing order, were slightly less efficient. On the other hand the main modification of the light signal produced by superoxide dismutase, desferrioxamine and myoglobin was characterized by a decrease of the luminescence during the course of the reaction. The reaction luminol-SIN-1 was compared with the known luminol-ABAP (2,2'-azo-bis-2-amidinopropane) method for evaluation of antioxidant capacity in human plasma, since this biological fluid modifies the luminol-SIN-1 reaction with well-defined induction times. Samples were obtained from patients with sepsis, a condition where it has been postulated that excess oxygen radicals including peroxynitrite are produced. Using Trolox as reference, the results (mean +/- standard error of mean) of both assays showed that the patients (SIN-1, 263 +/- 16; ABAP, 218 +/- 13; n = 19) have significantly (SIN-1, p < 0.02; ABAP, p < 0.001) lower values in comparison to non-septic controls (SIN-1, 330 +/- 16; ABAP, 398 +/- 16; n = 20). SIN-1 could be useful as a source of oxidant for the characterization of antioxidant behaviour in a system where superoxide and nitric oxide are simultaneously generated.

Antioxidants↗
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↗
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↗
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↗
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↗