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PubMed1995

Immunoaffinity column clean-up for the high-performance liquid chromatographic determination of aflatoxins B1, B2, G1, G2, M1 and Q1 in urine.

A method for the determination of aflatoxins B1, B2, G1, G2, M1 and Q1 in human urine has been developed. The 10-ml urine samples were automatically cleaned up on immunoaffinity columns and analysed by high-performance liquid chromatography (HPLC), including post-column derivatization with bromine and fluorescence detection. Average aflatoxin recoveries were: B1 103%, B2 106%, G1 98% and G2 96% in the range 6.8-73 pg/ml of urine and M1 103% and Q1 100% in the range 18-97 pg/ml of urine. The relative standard deviations were all between 1% and 21%. The determination limits of aflatoxins in urine were 6.8 pg/ml for B1, B2, G1 and G2 and 18 pg/ml for M1 and Q1.

Aflatoxin B1↗

PubMed2003

Aflatoxin B1 and its interconverting metabolite aflatoxicol in milk: the situation in Mexico.

Between 1996 and 1998, 580 litres of milk in Mexico were surveyed for aflatoxin B(1) (AFB(1)) and its metabolite aflatoxicol (AFL), which are mutagenic and carcinogenic mycotoxins that interconvert AFB(1)-AFL-AFB(1). The seven most consumed brands from different regions of Mexico included pasteurized and ultrapasteurized milk with four different fat levels: whole fat (28-33 g l(-1)), half-skimmed (10-20 g l(-1)), light (1-4 g l(-1)) and with vegetable oil (33 g l(-1)). Aflatoxins in each sample were concentrated with total aflatoxin immunoaffinity columns and quantitated by high-performance liquid chromatography. A milk sample was considered contaminated if it contained >/=0.05 microg l(-1) AFL. Pasteurization and ultrapasteurization of milk did not control contamination with AFL, which was present in 13% of samples at >/=0.05 microg l(-1) and in 8% at >/=0.5 microg l(-1), with a range of AFL from 0 to 12.4 microg l(-1). AFB(1) was present mainly in traces (0-0.4 microg l(-1)). The safest milk in relation to AFL contamination was imported milk powder with vegetable oil. There was a significant correlation between contamination of milk with AFL and the autumn (p<0.0002); the fat content was not significant.

Aflatoxin B1↗

PubMed2006

A simple steady-state model for carry-over of aflatoxins from feed to cow's milk.

A simple steady-state model is derived from two kinetic one-compartment models for the disposition of aflatoxin B1 (AFB1) and aflatoxin M1 (AFM1) in the lactating cow. The model relates daily intake of AFB1 in feed of dairy cattle and the cow's lactation status to resulting concentrations of AFM1 in milk. Moreover, assuming a linear relationship between the cow's lactation status and feed intake, the model relates daily milk production and AFB1 concentration in total feed to AFM1 levels in milk. The model explains similar experimental outcomes from different investigations into carry-over of aflatoxins from feed to milk. Although it is difficult to set a permanent limit for AFB1 in feed, the European Union (EU) limit of 5 microg AFB1 kg(-1) concentrate has proved, thus far, to be an appropriate level in preventing the EU limit of 0.05 microg AFM1 kg(-1) milk being exceeded.

Aflatoxin B1↗

PubMed1990

Biotransformation of aflatoxin B1 in rabbit lung and liver microsomes.

Aflatoxin B1 (AFB1) is a potent hepatotoxic and hepatocarcinogenic mycotoxin that requires bioactivation to AFB1-2,3-oxide for activity. In addition to epoxidation, microsomal monooxygenases biotransform AFB1 to the less toxic metabolites, aflatoxin M1 (AFM1) and aflatoxin Q1 (AFQ1). The lung is at risk from AFB1 both via inhalation and via the circulation. In the present study, we have characterized rabbit lung and liver microsomal AFB1-DNA binding (an index of AFB1-2,3-oxide formation), AFM1 formation and AFQ1 formation. Vmax values for AFB1-DNA binding were not different between lung and liver when expressed per mg microsomal protein (1.06 +/- 0.13 and 2.12 +/- 1.30 nmol/mg/h for lung and liver respectively), but lung values were greater than liver when expressed per nmol cytochrome P450 (3.64 +/- 0.31 and 1.29 +/- 0.70 nmol/nmol P450/h for lung and liver respectively). Km values for this reaction were not different between lung and liver. Vmax values for AFM1 formation in liver microsomes were greater than in lung when expressed per mg protein, but not when expressed per nmol P450. No differences were detected for the Km for AFM1 formation between lung and liver microsomes. For AFQ1 formation, no differences were detected between Vmax values of lung and liver, regardless of whether results were expressed per mg protein or per nmol P450, while the Km for AFQ1 formation was lower in liver. SKF-525A inhibited these reactions by 63-74% in lung microsomes and 90-96% in liver microsomes. These results indicate that the lung is capable of activating AFB1, and that rabbit lung microsomes contain high activity for this reaction. Furthermore, little AFM1 and AFQ1 are formed in lung microsomes, leading to minimal shunting of AFB1 from the activation pathway.

Aflatoxin B1↗

PubMed1991

Immunological and HPLC detection of aflatoxin adducts in human tissues after an acute poisoning incident in S.E. Asia.

Acid hydrolysed, purified DNA, extracted from formalin fixed human tissues from persons acutely exposed to aflatoxins during a poisoning incident, was found to inhibit antibody binding in a competitive aflatoxin inhibition ELISA both before and after immunoaffinity column purification. HPLC analysis of acid hydrolysates of the DNA revealed a peak with a retention time 3 min earlier than 8,9-dihydro-2-(N7-guanyl)-9-hydroxy AFB1 synthesized either by peracid activation or direct reaction of the 8,9-oxide with DNA. The major peak seen when DNA was extracted from formalin fixed tissues from rats treated with aflatoxin B1 was identical to that seen in the formalin fixed human tissues. Adduct levels ranged from 0 to 170 x 10(6) nucleotides depending on tissue type and individual examined.

Adolescent↗

PubMed1989

2(3)-tert-butyl-4-hydroxyanisole inhibits oxidative metabolism of aflatoxin B1 in isolated rat hepatocytes.

Previous studies indicate that dietary administration of phenolic antioxidants, 2(3)-tert-butyl-4-hydroxyanisole (BHA) and 3,5-di-tert-butyl-4-hydroxytoluene, inhibits the carcinogenic effect of a number of chemical carcinogens including aflatoxin B1 (AFB1). Induction of hepatic enzymes, such as glutathione S-transferase, UDP-glucuronyltransferase, and epoxide hydrolase, has been shown to be responsible for the reduction of AFB1 cytotoxic and carcinogenic effects. The effect of BHA on AFB1 activation was examined in vitro utilizing isolated rat hepatocytes and liver microsomes. In hepatocytes, the total AFB1 content and bound form of AFB1 were 3.4 and 1.4 pmol/10(6) cells, respectively. In the cell-free microsomal activating system, 2.2 pmol were activated per mg of microsomal protein during 60 min of incubation. BHA (0.1-0.5 mM) inhibited AFB1 activation and binding in both systems in a dose-dependent manner; in hepatocytes, 90% inhibition was observed at 0.5 mM. Analyzing various AFB1 adducts, BHA (0.25 mM)-treated hepatocytes contained a significantly reduced amount of AFB1 macromolecular adducts. The antioxidant neither stimulated nor inhibited the cytosolic glutathione S-transferase and microsomal UDP-glucuronyltransferase activities. Analysis of various hydroxylated (aflatoxins M1 and Q1 (AFM1 and AFQ1] and demethylated (aflatoxin P1 (AFP1] metabolites of AFB1 in both the conjugated and unconjugated form indicated that there was a 30-50% reduction of unconjugated AFP1, AFQ1, and AFM1, whereas AFB1 was increased 3-fold. There was no significant change of conjugated metabolites. The effect of BHA on AFB1 activation in hepatocytes was compared with that of other cytochrome P-450 inhibitors; the ED50 values of SKF 525A, BHA, and metyrapone were 9 microM, 40 microM, and 280 microM, respectively. In the cell-free microsomal system, biotransformation of AFB1 to AFP1, AFM1, and AFQ1 was also inhibited. Kinetic analysis of p-nitroanisole O-demethylase activity of rat liver microsomes demonstrated that BHA inhibited noncompetitively with an apparent Ki of 90 microM. In the absence of enzyme induction, the phenolic antioxidant, BHA, blocks the oxidative biotransformation of AFB1 in isolated hepatocytes.

Aflatoxin B1↗

PubMedDate not supplied

Determination of aflatoxicol and aflatoxins B1 and M1 in eggs.

Procedures from 2 methods, one for aflatoxins B1 and M1 in eggs and one for aflatoxicol in milk, blood, and liver, have been combined to determine the 3 toxins in eggs. The sample is blended with sodium chloride-saturated water and this mixture is then blended with acetone. After separation from the solid residue, the aqueous acetone extract is defatted with petroleum ether. The toxins are next partitioned into chloroform and separated from interferences on a silica gel column. Aflatoxicol is determined by fluorescence measurement after separation on a C18 reverse phase liquid chromatographic column, and aflatoxins B1 and M1 are determined by fluorescence densitometry after separation on a silica gel thin layer chromatographic plate. In a recovery study with eggs, mean recoveries of aflatoxicol added at levels of 0.1, 0.05, and 0.025 ng/g were 87, 77, and 78%, respectively. Mean recoveries of aflatoxins B1 and M1 added at a level of 0.1 ng/g were 75 and 87%, respectively, and at an added level of 0.05 ng/g were 86 and 75%. The within-laboratory precision (repeatability) ranged from 2 to 13%.

Aflatoxin B1↗

PubMed1998

Selection of a Suitable Method for Analysis of Aflatoxins in Date Fruits.

Fruits of the date palm (Phoenix dactylifera L.) are a vital component of the diet in most of the Arabian countries, but whether dates in the market are contaminated with aflatoxins is unknown. As screening will depend on accurate detection, the available AOAC Methods-with slight modification-for the recovery of aflatoxins were examined. The Romer minicolumn method failed to detect any aflatoxin in contaminated date fruits. Using the HPLC and postcolumn derivatization procedure, the contaminants branch (CB) method was found to give average recoveries of 75.7 and 83.5% for date varieties Lulu and Naghal, respectively. The recovery of total aflatoxins by the Best Food (BF) extraction and purification method was about 35% less than with the CB method.

Journal Article↗

PubMed1995

Demonstration of aflatoxin inhibitory activity in a cotton seed coat xylan.

An inhibitor of aflatoxin biosynthesis localized in the seed coats of developing cotton was partially purified and characterized. Aqueous extracts from 25-day postanthesis seed coat tissue inhibited aflatoxin (B(inf1)) production in liquid cultures of Aspergillus flavus AF13. Inhibition was concentration dependent, with a 50% effective dose of 173 (mu)g of crude extract per ml of medium. The inhibitor was neutral in charge. Two active fractions were obtained from crude preparations by gel filtration chromatography (BioGel P-100). The purest fraction eluted in the void volume. Carbohydrate composition analysis of this void volume inhibitor indicated a composition of xylose (>90%) and mannose. Aflatoxin production in vitro was inversely related to inhibitor concentration in the fermentation medium (log of aflatoxin versus log of [inhibitor]; r(sup2) = 0.82; P < 0.002). The void volume inhibitor had a 50% effective dose of 6.2 (mu)g/ml, a 28-fold purification of the inhibitor material. These data support the hypothesis that seed coat inhibitory activity is associated with a cottonseed-specific xylan.

Journal Article↗

PubMed1966

Microbial detoxification of aflatoxin.

Yeasts, molds, bacteria, actinomycetes, algae, and fungal spores were screened for their ability to degrade aflatoxin. Some molds and mold spores partially transformed aflatoxin B(1) to new fluorescing compounds. Only one of the bacteria, Flavobacterium (aurantiacum?) NRRL B-184, removed aflatoxin from solution. Both growing and resting cells of B-184 took up toxin irreversibly. Toxin-contaminated milk, oil, peanut butter, peanuts, and corn were completely detoxified, and contaminated soybean was partially detoxified by addition of B-184. Duckling assays showed that detoxification of aflatoxin solutions by B-184 was complete, with no new toxic products being formed.

Journal Article↗

PubMed1965

Effect of Aflatoxin B(1) on Cell Cultures.

Gabliks, J. (Massachusetts Institute of Technology, Cambridge), W. Schaeffer, L. Friedman, and G. Wogan. Effect of aflatoxin B(1) on cell cultures. J. Bacteriol. 90:720-723. 1965.-Aflatoxin B(1), a metabolite of the mold Aspergillus flavus, is toxic to cell cultures. The toxic effect is evidenced by an inhibition of growth followed by progressive granulation, rounding, and finally sloughing of the cells from the glass. In studies with embryonated eggs, duck embryos were found to be four to five times more susceptible than chick embryos. In studies on Chang liver cultures, there were decreases in cell number, protein, ribonucleic acid (RNA), and deoxyribonucleic acid (DNA) per culture with increasing aflatoxin B(1) concentrations. Since the cell number decreased and the protein, RNA, and DNA content per cell increased with increasing concentrations of aflatoxin, enlarged cells were suggested. These data are consistent with in vivo data of other workers who have found hypertrophic cells with enlarged nuclei in histological studies on the tissues of rats and ducklings fed toxic peanut meal.

Journal Article↗

PubMed1980

Rapid method for analysis of aflatoxin M1 in dairy products.

Four methods for determining aflatoxin M1 levels in fluid milk were compared in a search for a simple, routine analytical procedure.. Each method was tested with samples spiked at levels of 0, 0.1, 0.5, and 1.0 ppb. The 3 quantitative methods were comparable in sensitivity (0.1 ng/mL) and recoveries (80-90%). A new method, using a commercially available extraction column that contains an inert hydrophilic matrix to permit extraction of dairy products, is described. The milk is adsorbed on the column and aflatoxin M1 is eluted with chloroform-acetone (9 + 1). The extract is further purified on a small silica gel column and aflatoxin M1 is determined by TLC. This method was simpler and shorter, and was equally sensitive and reproducible in determining aflatoxin M1 in spiked and naturally contaminated fluid milk samples and in spiked nonfat powdered, condensed, and evaporated milk.

Chromatography, Thin Layer↗

PubMed1983

[Determination and occurrence of aflatoxin M1 in milk and dried milk products].

Basing on a review of the present situation of the contamination of milk and powdered milk products with aflatoxin M1 a further investigation is regarded as necessary to assess the hygienic toxicological situation. For this purpose the TLC detection method of Tuinstra and Bronsgeest is recommended, which was modified to be used with powdered milk and baby food. This method enables the detection of 0.04 micrograms M1/l milk and 0.5 micrograms/kg powdered milk respectively on practical conditions. Investigating 142 raw milk samples and 70 samples of powdered milk products only 2 positive powdered milk samples were detected. This relatively low contamination rate is explained by the use of feed that is predominantly produced in the GDR and that is vastly free from aflatoxins. According to these results it is possible to estimate the contamination of milk with aflatoxin M1 in the GDR as extremely low.

Aflatoxin M1↗

PubMed1997

Aflatoxin exposure is higher in vegetarians than nonvegetarians in Thailand.

Aflatoxin-albumin (AFB-albumin) adducts and hepatitis B markers (anti-HBs, and anti-HBc) were measured in vegetarians and nonvegetarians from Chiang Mai, Thailand. The AFB-albumin adduct levels were detected in 62% (37 of 60) of the vegetarian samples and 22% (22 of 100) of nonvegetarians. Somewhat higher levels were detected in vegetarians sera collected in the summer than in the winter, although this difference was not statistically significant. Subjects who were hepatitis B surface antigen (HBsAg)-positive had slightly higher AFB-albumin adduct levels than subjects who had evidence of past exposure (anti-HBc-positive) or no HB virus infection. This study indicated that vegetarians may have a higher frequency of aflatoxin exposure than nonvegetarians. Thai vegetarians consume various vegetables, grains, peanut, soybean, and fermented products, which have been reported to be sources of aflatoxin.

Adolescent↗

PubMed1997

CYP1A induction by beta-naphthoflavone, Aroclor 1254, and 2,3,7,8-tetrachlorodibenzo-p-dioxin and its influence on aflatoxin B1 metabolism and DNA adduction in zebrafish.

This study investigated the inductive response of cytochrome P4501A (CYP1A) in the zebrafish (Danio rerio) following exposure to Aroclor 1254, beta-naphthoflavone (betaNF), and 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) and then investigated TCDD modulation of aflatoxin B1 (AFB1) metabolism and hepatic AFB1-DNA adduction. Aroclor 1254 fed at 500 ppm for 1 to 9 days or intraperitoneal (ip) injection of 75-200 mg Aroclor 1254/kg body weight failed to induce CYP1A protein or associated 7-ethoxyresorufin-O-deethylase (EROD) activity. By contrast, dietary betaNF at 500 ppm for 3 or 7 days induced CYP1A protein and EROD activity approximately threefold above controls. A single ip injection of 150 mg/kg betaNF showed maximal induction of CYP1A protein and EROD activity near 24 hr, both of which decreased to control levels during the next 6 days. Single ip administration of 25, 50, 100, or 150 mg betaNF/kg body weight provided dose-responsive increases in CYP1A and EROD activity. Dietary exposure to 0.75 ppm TCDD for 3 days also significantly induced CYP1A and EROD. The effect of TCDD on the metabolism of [3H]AFB1 in zebrafish was then investigated. The major [3H]AFB1 metabolites excreted in water over 24 hr in the control group were aflatoxicol, aflatoxicol-glucuronide, and parent AFB1. By contrast, the predominant metabolites in the TCDD-pretreated group were aflatoxicol-M1-glucuronide, aflatoxicol, aflatoxin M1 plus aflatoxicol-M1 (unresolved), aflatoxicol-glucuronide, and parent AFB1. Surprisingly, hepatic AFB1-DNA adduction was approximately fourfold higher in the TCDD treated group than in controls. This significant difference could not be explained by increased capacity for bioactivation of AFB1 as measured by an in vitro AFB1-exo-8, 9-epoxide trapping assay. However, it was demonstrated that both control and induced zebrafish have high capacity to bioactivate aflatoxin M1 to a reactive intermediate, such that secondary bioactivation of this genotoxic intermediate may be responsible for the increased DNA binding.

Aflatoxin B1↗

PubMed1998

Metabolism and toxicity of aflatoxins M1 and B1 in human-derived in vitro systems.

Aflatoxin M1 (AFM1) is the principal hydroxylated aflatoxin metabolite present in the milk of dairy cows fed a diet contaminated with aflatoxin B1, (AFB1) and the metabolite is also present in the milk of human nursing mothers consuming foodstuffs containing the toxin. AFM1 is usually considered to be a detoxification product of AFB1 and this appears warranted if the biological endpoints involved are carcinogenicity and mutagenicity. However, it may not be a valid conclusion in the case of cytotoxicity. The metabolism of AFM1 and AFB1 have been studied in vitro using human liver microsomes. Formation of primary metabolites associated with metabolic activation to the respective epoxides reflected the differences between the carcinogenic potentials of the two toxins and, similar to AFB1, the conjugation of AFM1 epoxide with reduced GSH was catalyzed by mouse, but not human liver cytosol. Although the majority of the binding of [3H]AFB1 to microsomal protein was dependent on metabolic activation, a high level of retention of [3H]AFM1 by microsomes, nonextractable in methanol and unrelated to metabolic activation, was observed. It appears possible that this property is related to the high cytotoxicity of AFM1. Experiments using human cell line cells either expressing or not expressing human cytochrome P450 enzymes in assays of acute toxicity (MTT assays) have demonstrated a directly toxic potential of AFM1 in the absence of metabolic activation, in contrast to AFB1. Caution therefore needs to be exercised in designating the formation of AFM1 as essentially detoxification when considering a biological response in which cytotoxicity may play a significant role, e.g., immunotoxicity.

Aflatoxin B1↗

PubMed1982

Development of Aspergillus parasiticus and formation of aflatoxin B1 under the influence of conidiogenesis affecting compounds.

The influence of various inhibitors of hyphal growth, sporulation and biosynthesis of aflatoxin B1 in Aspergillus parasiticus NRRL2999 was studied. 6-Thioguanine, DL-ethionine, fluoroacetic acid and phenylboric acid, inhibitors of maturation of fungal conidiophores and of conidiogenesis, were added at various concentrations to malt extract agar. Lower concentrations of 6-thioguanine and DL-ethionine did not inhibit the growth of hyphae and the sporulation. Phenylboric acid reduced conidiogenesis more than hyphal growth. The yields of aflatoxin B1 were significantly reduced. Additions of fluoroacetic acid did not greatly affect the growth of hyphae but totally inhibited the production of conidia and concurrently significantly reduced the formation of aflatoxin B1. An interrelation between conidiogenesis and onset of secondary metabolism in A. parasiticus is evident.

Aflatoxin B1↗

PubMed1988

Metabolic behaviour of aflatoxin producing strain and non-toxigenic strain of Aspergillus flavus to different sources of nitrogen and glucose concentration.

The effect of different nitrogen sources and varying glucose concentration on aflatoxin production by a toxigenic and non-toxigenic strain of Aspergillus flavus was studied. Greatest production (3.8 ppm) of aflatoxin B1 was produced in a synthetic medium when casamino acids were supplied as the nitrogen source. Optimum sugar concentration for aflatoxin B1 production ranged between 3 and 10 g/100 ml. There was no appreciable difference in the metabolic behaviour between toxigenic and non-toxigenic strains of A. flavus when dry mycelial weight, total proteins, non-protein nitrogen and reducing sugar were the criteria.

Aflatoxin B1↗