Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Aflatoxin B1”

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 505 records · Page 28Linked to original sources
PubMed1988

[Determination of aflatoxin B1 in dried figs by visual screening, thin-layer chromatography and ELISA].

Aflatoxin B1-contaminated fruits were sorted out from 250 kg dried figs (five Turkish and three Greek batches) by bright-greenish-yellow fluorescence under UV light. The aflatoxins of the fluorescent figs were extracted by simple soaking in methanol. Aflatoxin B1 was determined by thin-layer chromatography. Parallel to this, an extraction for the determination of aflatoxin B1 was developed by a competitive ELISA and the two methods were compared with each other. In a highly contaminated batch of Turkish figs, statistically there was one fig among 350 which had a high aflatoxin content (greater than 100 ng/g fig) and one fig amongst 140 fruits with an aflatoxin B1 content of greater than 10 ng B1/g fig.

Aflatoxin B1↗
PubMed1992

Comparison of the aflatoxin B1-8,9-epoxide conjugating activities of two bacterially expressed alpha class glutathione S-transferase isozymes from mouse and rat.

The complementary DNAs of rat glutathione S-transferase (GST, EC 2.5.1.18) Yc1 and of mouse Yc were expressed from a prokaryotic expression vector in E. coli. The purified proteins were analyzed for their activity toward aflatoxin B1-8,9-epoxide (AFBO), the reactive intermediate of the fungal mycotoxin aflatoxin B1 (AFB). The mouse Yc isozyme had about 50-fold higher conjugating activity toward AFBO than the rat Yc1 isozyme (144 nmol/mg/min versus 3.3 nmol/mg/min). The rat Yc1 isozyme had specific activities toward 1-chloro-2,4-dinitrobenzene, cumene hydroperoxide and ethacrynic acid of 10.7, 0.98 and 0.92 mumol/mg/min, respectively, whereas the mouse Yc isozyme had specific activities of 5.7, 2.1 and 0.1 mumol/mg/min for these substrates, respectively. These data provide further support for the hypothesis that the constitutive presence of the alpha class GST Yc isozyme in mouse liver protects mice from the hepatocarcinogenic effects of aflatoxin B1.

Aflatoxin B1↗
PubMed1991

The isolation and culture of DHBV-infected embryo and duckling hepatocytes and the effect of aflatoxin B1 or irradiation on these cells.

The preparation of primary cultures of control and DHBV-infected duck hepatocytes from embryos and young ducklings is described. Cultures of both embryo and duckling hepatocytes secreted duck serum proteins. Cultures of hepatocytes established from ducklings maintained initial morphology for up to 3 weeks in culture and also exhibited high levels of metabolism of aflatoxin B1. Embryonic cell cultures rapidly lost ability to metabolise AFB1 and became overgrown by spindle-shaped cells. Both embryo and duckling cell cultures secreted infective DHBV, and had intracellular replicative forms of the virus. No integration of the virus into the duck genome was observed, and attempts to induce viral integration in the duckling hepatocytes using irradiation and aflatoxin B1 toxicity were unsuccessful. The results of the study lend further support to the suggestion that the rarity of liver cancer in DHBV-infected experimental ducks is related to an innate resistance of the hepatocytes to develop DHBV-DNA integration. Another possibility may be related to the lower oncogenic potential of the DHBV strain used for the study. However DHBV infected duckling hepatocytes would appear to offer a suitable material for studying viral replication and mechanisms of aflatoxin B1 toxicity during prolonged cell culture.

Aflatoxin B1↗
PubMed1980

Influence of gamma irradiation of aflatoxin B1 production by Aspergillus flavus growing on some Nigerian foodstuffs.

Spores of Aspergillus flavus (UI, 81) inoculated into some local food materials were irradiated at 62.5, 125.0, 250.0 and 500.0 krad, and the effect on aflatoxin B1 production on subsequent incubation was measured. The results show that aflatoxin B1 production decreased with increasing gamma irradiation dose in soya bean, groundnut, palm juice, while paw paw mash showed a relatively high yield of aflatoxin at 125.0 krad as compared to other irradiation levels tested except for the control. Irradiation of soya bean and groundnut inoculated with spores of Aspergillus flavus at 500.0 krad (pre-irradiation incubation period of 2 h) inhibited aflatoxin B1 production. Analysis of variance showed that media, pre-irradiation incubation periods and irradiation levels affected the total amounts of aflatoxin produced.

Aflatoxins↗
PubMed2006

Determination of aflatoxin B1 in tiger nut-based soft drinks.

An analytical method for the determination of aflatoxin B1 in a tiger nut-based soft drinks named 'horchata' is described. The method is based on an immunoaffinity clean-up, followed by HPLC separation and fluorescence detection after electrochemical post-column derivatization. The detection limit (S/N = 3) and the quantification limit (S/N = 10) were 0.02 and 0.06 microg kg(-1), respectively. The mean recovery at a level of 2 microg l(-1) was 88% (n = 6) and the coefficient of variation was 9%. The method was applied to conduct a small market survey for a beverage named 'horchata' that is frequently consumed by parts of the population in Southern Europe. Twenty-two samples from Spanish and Belgian supermarkets were analysed. As a result, only one sample was found to contain aflatoxin B1 at the limit of quantitation of the method.

Aflatoxin B1↗
PubMed1975

Interaction of aflatoxin B1 with DNA.

The interaction of aflatoxin B1 with DNA was investigated. In the presence of native DNA the absorption spectrum of the toxin showed an obvious spectral shift in the region of 300-420 nm with an isosbestic point at 376 nm. DNA-bound aflatoxin is hydrolyzed in alkaline media more easily than the free toxin. The hydrolized form has a labile structure and can decompose further. The bound toxins are easily dissociated by heat as well as by salt, and all toxin molecules are released from DNA which remains double-stranded. Aflatoxin can bind to thermally denatured DNA as well, with an accompanying spectral shift which depends on the particular preparation of denatured DNA, and there was an isosbestic point at 380 nm. The complex of toxin and denatured DNA was stabilized by salt up to 0.1 M. Thus it was concluded that aflatoxin was bound with denatured DNA in a different form from native DNA. The number of binding sites of DNA was estimated by constructing Scatchard plots based on both spectral analysis and equilibrium dialysis. However, these show no definite value but fall in the region of 0.07 to 0.013, that is one toxin molecule per 80-140 nucleotide of native DNA. Several lines of evidence suggest the possibility that aflatoxin exists in aqueous solution as aggregates. The mechanism of the binding was discussed. It is noteworthy that the number of binding sites of DNA doubles by the presence of histones.

Aflatoxins↗
PubMed1979

Laser fluorometric determination of aflatoxin B1 in corn.

A 2-step chromatographic separation, using both thin layer chromatography (TLC) and high pressure liquid chromatography (HPLC), in conjunction with the high sensitivity of laser fluorometry permits extension of the detection limits of aflatoxin contamination in corn to 0.1 ppb (microgram/kg) with a 26% root mean square variation. Aflatoxin B1 is extracted from corn with water-methanol and cleaned up by TLC. The recovery of aflatoxin from the TLC plates was linear from 10 to 1000 pg. Aflatoxin B1 is converted to the more highly fluorescent B2A derivative by treatment with 1N HCl. Experiments with aflatoxin B1 standard establish a constant conversion to B2A over approximately 3 orders of magnitude in B1 concentration. An extract of the B2A aflatoxin derivative is injected onto a reverse phase HPLC column. A flowing droplet of eluant is irradiated by an amplitude-modulated 325 nm He-Cd ion laser beam, and fluorescence from the droplet is detected by a lock-in amplifier in phase with the laser modulation. Several chromatograms are presented that demonstrate the capability of this procedure for removing interfering components in the corn extract.

Aflatoxins↗
PubMed1991

A light & electron microscopic study on apoptotic bodies in acute aflatoxin B1 induced injury in the rat liver.

A subnecrogenic dose of aflatoxin B1 (AFB1) was injected intraperitoneally into 8-10 wk old male rats of the Holzman strain. Cytoplasmic and sinusoidal eosinophilic bodies were seen in the liver which appeared at 30 h and reached a maximum at 48 h. Electron microscopically some of the cytoplasmic structures were seen to be of mitochondrial origin whereas others resembled apoptotic bodies. The sinusoidal bodies were similar to apoptotic bodies.

Aflatoxin B1↗
PubMed2001

Effect of an extract of the root of Scutellaria baicalensis and its flavonoids on aflatoxin B1 oxidizing cytochrome P450 enzymes.

The inhibition of aflatoxin B1 (AFB1) metabolism by a water extract of the root of Scutellaria baicalensis and its flavonoids was examined in liver microsomes. AFB1 is known to be metabolized to aflatoxin M1 (AFM1), aflatoxin Q1 (AFQ1), and AFB1-8,9-epoxide (AFBO). The water extract potently inhibited the production of AFM1 by cytochrome P450 (CYP)1A1/2 and slightly reduced AFBO formation by CYP1A1/2, CYP2B1, CYP2C11 and CYP3A1/2 in TCDD-treated rat liver microsomes. IC50 values for AFM1 and AFBO formation were 6.8 and 122.4 microg/ml, respectively. Wogonin showed the highest inhibitory activity towards AFM1 formation among the flavonoids isolated from the extract. On the other hand, the extract had no effects on the formation of AFBO and AFQ1 in human liver microsomes, and on the activities of CYP2B1, CYP2C11 and CYP3A1/2 which were detected by hydroxylation patterns of testosterone. These results demonstrated that the extract of the root of Scutellaria baicalensis has a specific inhibitory effect on CYP1A1/2 among CYP enzymes involved in AFB1 metabolism by rat and human microsomes.

Aflatoxin B1↗
PubMed1989

Enzymes in aflatoxin B1 biosynthesis: strategies for identifying pertinent genes.

Recent work on the aflatoxin biosynthetic pathway is reviewed, with special emphasis on the enzymes of the late stages of the pathway involving conversion of sterigmatocystin (ST) to aflatoxin B1 (AFB1) through an O-methylsterigmatocystin intermediate. Two enzyme activities were discovered in subcellular fractions of cell-free extracts of a mutant strain of Aspergillus parasiticus (SRRC 163): 1) A post-microsomal methyltransferase (MT) catalyzed conversion of ST to OMST, and 2) a microsomal-associated activity (oxido-reductase) converted OMST to AFB1. The 168 KDa, anionic MT was purified to homogeneity and characterized (two subunits, 110 KDa and 58 KDa). Preliminary evidence indicated the presence of a cationic isozyme of the MT in mycelial extracts. The oxido-reductase has been partially purified and characterized. Polyclonal antibodies were prepared to the anionic MT and the enzyme's amino acid composition determined. A cDNA library has been constructed from mRNA isolated from Aspergillus parasiticus mycelia during the onset of AFB1 biosynthesis for the purpose of identifying the genes responsible for aflatoxin biosynthesis.

Aflatoxin B1↗
PubMed1983

Induction of retrovirus gene expression by aflatoxin B1 and 2-acetylaminofluorene.

The abilities of 2-acetylaminofluorene (AAF) and aflatoxin B1 (AFB) to induce the expression of endogenous murine retrovirus in AKR mouse embryo fibroblasts were examined. AFB was able to induce virus expression at concentrations as low as 0.067 microM, although the induction efficiency was increased at higher doses. AAF gave somewhat more variable results. In some experiments induction was observed with as little as 0.1 microM while in other experiments induction was not observed at concentrations as high as 100 microM. Addition of an S9 metabolizing system enhanced the ability of AAF to induce virus expression but also increased the background induction frequency. These results are discussed in relation to the mechanism of virus induction and the potential usefulness of virus induction as an assay for carcinogenic potential.

2-Acetylaminofluorene↗
PubMed1991

The effect of partial hepatectomy on the genotoxicity of aflatoxin B1.

The influence of partial hepatectomy on the genotoxic effect of aflatoxin B1 (AFB1) mycotoxin in male Chinese hamsters (Cricetulus griseus) was studied after application of a single i.p. dose of 1.0 mg AFB1/kg. Changes in the fractions of proliferating bone marrow cells, values of the mitotic index of liver cells and morphologic changes in liver tissue were also monitored. Partial hepatectomy reduced significantly the mutagenic activity of AFB1 measured by the frequency of chromosome aberrations in bone marrow cells during 5 days. In hepatectomized animals AFB1 cytotoxicity was significantly reduced as evaluated by changes in the values of proliferating bone marrow cell fractions. There were no important morphologic changes in the liver. In hepatectomized AFB1 treated animals mitotic activity in liver tissue was substantially lower than in hepatectomized but AFB1 untreated animals.

Aflatoxin B1↗
PubMed1981

Mutagenicity of aflatoxin B1: observations in vivo and their relation to in vitro activation.

Aflatoxin B1 (AFB1) was shown to be clastogenic in vivo on the basis of its capacity to produce micronucleated cells and chromosomal aberrations in mouse bone marrow cells. On the other hand, in vitro studies on cultured human lymphocytes suggested only a slight mutagenic action of AFB1. If, however, a microsomal extract isolated from rat liver was added together with the AFB1 (1.92 X 10(-5) M) to the lymphocytes before the incubation period, the yield of chromosomal aberrations and of sister chromatid exchanges (SCE) increased markedly indicating that AFB1 must be metabolically converted before it can act as an active mutagen. The use of microsomal extracts for in vitro tests can thus considerably improve the reliability of such tests of mutagenicity although studies in vitro will not be able to entirely replace those in vitro.

Aflatoxin B1↗
PubMed1982

Effects of sex difference and dietary protein level on the binding of aflatoxin B1 to rat liver chromatin proteins in vivo.

The risk of aflatoxin-induced hepatocarcinoma is greater in males than in females and is similarly higher in animals fed 20% casein diets than in those fed 5%. In this study, groups of male and female F344 rats were fed either a 5 or 20% casein diet for 6 weeks. Two hr after a 1-mg/kg i.p. dose of [3H]aflatoxin B1, animals were killed and four protein fractions were sequentially extracted from the liver chromatin of each. Within each treatment group, aflatoxin binding to nonhistones was greater than to histones, both before and after dialysis. Comparing treatments, the higher-risk factors were associated with a greater liver content of aflatoxin as well as with increased binding of both nondialyzable and dialyzable aflatoxin to the various fractions. The high degree of correlation between total liver content and adduct formation implicates the former as a major determinant of the latter. Also associated with the higher-risk factors was a shift in the distribution of dialyzable aflatoxin toward greater adduct formation with one of the nonhistone fractions, suggesting the possibility of a role for noncovalent aflatoxin:protein adducts in hepatocarcinogenesis.

Aflatoxin B1↗
PubMed1988

Reduction of mutagenicity and toxicity of aflatoxin B1 by chlorine gas treatment.

Chlorine gas was used to treat aflatoxin B1 (AFB1). The time-related exposure study showed that 4 ml (15 mg) pure chlorine gas caused about 90% destruction of 100 micrograms AFB1 within 10 min, at standard temperature and pressure. Four fluorescent reaction products were produced, two of which were identified as 8,9-dichloro-AFB1 and 8,9-dihydroxy-AFB1 (diol). The use of [14C]AFB1 confirmed the 90% destruction of the compound by chlorine gas. An increased destruction of AFB1 also occurred when an increased amount of chlorine gas was used. The mutagenic activity of the AFB1 sample treated for 10 min was reduced to about 5% of the untreated control using the Salmonella typhimurium strain TA98 in the presence of a rat-liver S-9 mix. A similar time-related reduction in AFB1 toxicity after chlorine treatment was also achieved using the chicken embryo toxicity assay.

Aflatoxin B1↗
PubMedDate not supplied

Long term administration of low doses of mycotoxins in poultry. 2. Residues of ochratoxin A and aflatoxins in broilers and laying hens after combined administration of ochratoxin A and aflatoxin B1.

The effects of combined administration of ochratoxin A (OA) and aflatoxin B1 (AFB1) on the occurrence and the levels of residues of mycotoxins in poultry have been investigated. Male broilers and laying hens were fed from 14 days old with standard diets contaminated with 50 micrograms/kg OA and 50 micrograms/kg AFB1. Two groups of broilers and hens were withdrawn from contaminated feed at 37 and 88 days, respectively. At the time of sacrifice no significant lesions were found. Residues were compared with those found after administration of either toxin alone in former trials. Combined treatment resulted in higher content of OA in broiler livers (40 versus 5.0 micrograms/kg) and, to a lesser extent, in kidneys and skin, and of AFB1 in broiler liver and kidney (0.15 versus 0.02 microgram/kg and 0.40 versus 0.05 microgram/kg respectively). Laying hens showed smaller differences (0.20 versus 0.10 microgram/kg in liver and 0.32 versus 0.08 in kidneys). Withdrawal from treatment led to the almost complete disappearance of OA residues in broilers and in hens. These results show a synergistic effect of OA and AFB1, particularly in broilers.

Aflatoxin B1↗
PubMed1991

Effects of crocetin on the hepatotoxicity and hepatic DNA binding of aflatoxin B1 in rats.

The effects of crocetin pretreatment on both hepatic aflatoxin B1 (AFB1)-DNA binding and AFB1 hepatotoxicity in rats has been examined. For these studies, male Wistar rats were treated with AFB1 (2 mg/kg) by i.p. administration, and the different degrees of hepatic damage were revealed by the elevations of levels of serum marker enzymes such as aspartate aminotransferase, alanine aminotransferase, lactate dehydrogenase and gamma-glutamyltranspeptidase. After pretreatment of the animals with crocetin (2 or 6 mg/kg) daily for three consecutive days, the enzyme elevations were significantly suppressed. This suggested that the crocetin possessed chemopreventive effects on the early acute hepatic damage induced by AFB1. Under these experimental conditions, consistent elevations of hepatic glutathiones (GSH) and activities of glutathione S-transferase (GST) and glutathione peroxidase (GSH-Px) were observed. Crocetin treatment also decreased AFB1-DNA adduct formation in AFB1-treated animals. From these results, we suggest that the protective effect of crocetin on AFB1 hepatotoxicity in rats might be due to the hepatic tissues' defense mechanisms that elevated the cytosol GSH and the activities of GST and GSH-Px.

Aflatoxin B1↗
PubMed1991

Aflatoxin B1 alters central and systemic tryptophan and tyrosine metabolism: influence of immunomodulatory drugs.

Semi-chronic exposure of ICR male Mice to Aflatoxin B1 (AFB1) in non-toxic doses results in elevated lung tryptophan (TRP) levels without change in serotonin (5-HT) or 5-hydroxyindole-3-acetic acid (5-HIAA) levels. This change is organ specific in that TRP levels are not altered in spleen, duodenum, heart or central nervous system (CNS). Acute (48 hour) flunixin treatment decreases lung TRP levels and reverses the AFB1 mediated increase in lung TRP levels. On the other hand, flunixin treatment decreases CNS TRP levels in control mice but not in AFB1 treated mice. Aflatoxin B1 treated mice have an increase in splenic serotonin (5-HT) content. Acute (48 hour) treatment of mice with E. coli lipopolysaccharide (LPS) also increases splenic 5-HT, and AFB1 treatment followed by LPS have a slightly additive effect on spleen 5-HT content. Treatment of mice with LPS increases heart 5-HT, an effect which is not altered in AFB1 pretreated mice. Both LPS and AFB1 per se increases lung TYR levels although the combination of treatments is not significantly different from the control value. Flunixin treatment increases lung tyrosine (TYR) levels, an effect which is not altered by AFB1 pretreatment. Acute treatment with either LPS or flunixin decreases the CNS TRP/TYR ratio; pretreatment with AFB1 prevents those changes in the CNS TRP/TYR ratio. Central nervous system catecholamines are reduced in AFB1 pretreated mice. However, CNS catecholamine changes in AFB1 treated mice are normalized by vitamin E supplementation during the treatment period.

Aflatoxin B1↗