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PubMed1987

A survey of urinary aflatoxin in Zimbabwe.

In this study, 1228 urine samples were collected from different centres in Zimbabwe and were analysed for aflatoxin contamination. The urine samples were extracted with chloroform and analysed by thin layer chromatography and high-performance liquid chromatography. The most commonly observed contaminant was aflatoxin M1, at an average concentration of 4.2 ng/ml of urine. Although the national average of urine samples contaminated was 4.3%, there were areas in which up to 10% of the urine samples were contaminated.

Aflatoxins↗

PubMed1995

Inhibition of CYP1A2 and CYP3A4 by oltipraz results in reduction of aflatoxin B1 metabolism in human hepatocytes in primary culture.

Dithiolethiones are thought to act as potent chemoprotective agents against aflatoxin B1 (AFB1)-induced hepatocarcinogenesis in the rat by inducing glutathione S-transferases (GSTs). To determine whether these antioxidants can be similarly effective in human beings, we have investigated metabolism of AFB1, in primary human hepatocytes with or without pretreatment by oltipraz (OPZ), a synthetic derivative of the natural 1,2-dithiole-3-thione. Aflatoxin M1 (AFM1), glutathione conjugates of AFB1 oxides (AFBSGs), and unchanged AFB1 were quantitated in cultures derived from eight human liver donors. Parenchymal cells obtained from the three GST M1-positive livers metabolized AFB1 to AFM1 and to AFBSGs derived from the isomeric exo-and endo-8,9-oxides, whereas no AFBSGs were formed in the GST M1-null cells. Pretreatment of the cells with 3-methylcholanthrene or rifampicin, inducers of CYP1A2 and CYP3A4, respectively, caused a significant increase in AFB1 metabolism. Although OPZ induced GST A2, and to a lesser extent GST A1 and GST M1, it decreased formation of AFM1 and AFBSG, which involves CYP1A2 and CYP3A4. Inhibition by OPZ of AFB1 metabolism by reducing CYP1A2 and CYP3A4 was also demonstrated by decreased activity of their monooxygenase activities toward ethoxyresorufin and nifedipine, respectively. The significant inhibition by OPZ of human recombinant yeast CYP1A2 and CYP3A4 was also shown. These results demonstrate that AFBSG can be formed by GST M1-positive human hepatocytes only, and suggest that chemoprotection with OPZ is due to an inhibition of activation of AFB1, in addition to a GST-dependent inactivation of the carcinogenic exo-epoxide.

Aflatoxin B1↗

PubMed1982

Effect of cyclopropenoid fatty acids on the hepatic microsomal mixed-function-oxidase system and aflatoxin metabolism in rabbits.

Male New Zealand weanling rabbits were fed a diet containing 0.25% cyclopropenoid fatty acids for 28 days. Compared with the controls, the rabbits given cyclopropenoid fatty acids showed retarded growth, some moderate liver histological damage, altered hepatic mixed-function-oxidase activities and minor variations in vitro [14C]aflatoxin B1 metabolism. In in vitro assays the major hepatic metabolite of aflatoxin B1 (AFB1) was aflatoxicol (AFL) and the major AFL metabolite was AFB1. Minor amounts of aflatoxin M1 and a metabolite believed to be AFL-M1 were formed. The similarity of this AFB1 metabolite pattern to that in rainbow trout, taken together with the apparent absence of AFB1 detoxification products is consistent with the sensitivity of both species to the acute effects of AFB1.

Aflatoxin B1↗

PubMed1997

Modulation of aflatoxin B1 carcinogenicity, genotoxicity and metabolism in rat liver by dietary carotenoids: evidence for a protective effect of CYP1A inducers.

The effects of several carotenoids of vitamin A and of 3-methylcholanthrene have been tested on the initiation of hepatocarcinogenesis by aflatoxin B1, using the sequential protocol of Solt and Farber. AFB1-induced DNA single-strand breaks and AFB1-metabolism were also assessed. The P4501A inducer carotenoids (canthaxanthin, astaxanthin, beta-apo-8'-carotenal) and 3-methylcholanthrene reduce the carcinogenicity of AFB1, divert AFB1-metabolism into the less genotoxic aflatoxin M1 and reduce AFB1-induced DNA single-strand breaks: we conclude that these carotenoids exert their protective effect through the deviation of AFB1 metabolism towards detoxification pathways. beta-Carotene decreased AFB1 carcinogenicity but did not alter its metabolism, probably acting by other mechanisms.

Aflatoxin B1↗

PubMed1990

Evidence for involvement of multiple forms of cytochrome P-450 in aflatoxin B1 metabolism in human liver.

Liver cancer is a major cause of premature death in many areas of Africa and Asia and its incidence is strongly correlated with exposure to aflatoxin B1 (AFB1). Because AFB1 requires metabolic activation to achieve a biological response, there is a need for detailed knowledge of the mechanism of activation to assess individual risk. We have carried out an extensive study using a total of 19 human liver samples to determine the individual variability in the metabolism of the toxin to mutagenic or detoxification products and to identify the specific cytochrome P-450 forms involved in these processes. Metabolism to the toxic 8,9-epoxide or to products mutagenic in the Ames test was found to exhibit very large individual variation. The rates of metabolic activation were highly correlated with both the level of proteins of the P450IIIA gene family and with the total cytochrome P-450 content of the microsomes. In agreement with this, antibodies reacting with P450IIIA proteins were strong inhibitors of both the metabolism and mutagenicity in the majority of the samples. However, the inhibition varied between 50% and 100%. The expression of a protein in the P450IIC gene family also correlated with AFB1 metabolism and mutagenicity. This result therefore indicated the involvement of cytochromes other than P450IIIA in the activation of AFB1 by human liver microsomes. This hypothesis was strongly supported by the finding that antibodies to P450IA2 and P450IIA1 were also effective inhibitors of metabolism in many of the samples. These data demonstrate that, although P450IIIA probably plays an important role in AFB1 activation, several other cytochrome P-450 forms have the capacity to activate the toxin. Similar considerations apply to detoxifying metabolism to aflatoxin Q1 and aflatoxin M1. The levels of expression of many of the forms of cytochrome P-450 involved in AFB1 metabolism are known to be highly sensitive to environmental factors. This indicates that such factors will be an important determinant in individual susceptibility to the tumorigenic action of AFB1.

Aflatoxin B1↗

PubMed2006

Molecular cloning and expression of a novel cytochrome p450 from turkey liver with aflatoxin b1 oxidizing activity.

Cytochromes P450 are members of a superfamily of oxidative hemoprotein enzymes that metabolize a variety of endogenous and exogenous compounds. Previous studies in our laboratory have shown that efficient P450-mediated activation underlies the extreme sensitivity of poultry, specifically turkeys, to the toxic effects of the mycotoxin aflatoxin B1 (AFB1). Using 3'- and 5'-rapid amplification of cDNA ends (RACE), we amplified from turkey liver RNA a full-length 1.73 kb cDNA predicted to be 528 amino acids with 94.7% sequence identity to a CYP1A5 from chicken liver. A truncated construct of the turkey CYP1A5 gene with 29 amino acids deleted from the hydrophobic NH2-terminal region was cloned and heterologously expressed in Escherichia coli. The expressed protein from E. coli membranes had a CO-binding spectrum typical of P450s, and it catalyzed the O-dealkylation of the CYP1A prototype substrates ethoxyresorufin and methoxyresorufin. CYP1A5-mediated O-dealkylation of methoxyresorufin was completely inhibited by alpha-naphthoflavone, a specific CYP1A inhibitor. Inhibitors to other mammalian P450s (3A4, 2D, 2E, and 3A1) either slightly inhibited this activity or not at all. CYP1A5 oxidized AFB1 to form two metabolites: the reactive intermediate, AFB1 -8,9-epoxide (AFBO), and aflatoxin M1 (AFM1). Because of the importance of AFBO and AFM1 in the toxicity of AFB1, we conclude that this P450 probably plays some role in the well-known hypersensitivity of turkeys to AFB1. To our knowledge, this is the first P450 cloned and sequenced from turkeys, the species in which the toxicity of AFB1 was first discovered.

Aflatoxin B1↗

PubMed1997

Evaluation of low-level aflatoxin in the diet of white-tailed deer.

We evaluated the response of white-tailed deer (WTD) (Odocoileus virginianus) to dietary aflatoxin. Fourteen 4-to-5-mo-old WTD were used in this 8-wk study, conducted between November 1993 and January 1994. Seven animals received a ration containing 800 parts per billion (ppb) total aflatoxin (AF). Seven control animals received the same ration without AF. At 0, 1, 3, 6 and 8 wk, feed consumption, feed conversion, liver enzymes, bile acid levels, and immune function via lymphocyte proliferation assays and delayed type hypersensitivity reactions were determined. At the conclusion of the 8-wk feeding trial, deer were euthanized and necropsied. Clinical illness was not evident in any of the animals, but by the end of the study, AF-fed deer had reduced feed consumption and body weight as compared to control deer; the differences were not statistically significant. The AF-exposed group had a significant increase (P = 0.03) in serum bile acid concentration as compared to control deer. Two AF-exposed deer had gross and histologic hepatic lesions indicative of a mild degenerative hepatopathy. Residues of an aflatoxin metabolite, aflatoxin M1, were found in the livers of all treated animals. No differences in immune function were detected between the two groups. We conclude that consumption of 800 ppb AF in the diet of young WTD over an 8-wk period can produce subclinical hepatic injury.

Administration, Oral↗

PubMed2000

[Relevance of mycotoxin contaminated feed for farm animals and carryover of mycotoxins to food of animal origin].

Contaminated feed is the main source for mycotoxin infestation of farm animals. The oral intake of fungal metabolites with feed results in a negative impact on all relevant parameters of animal production. Moreover, under experimental conditions mycotoxins and/or their metabolites can be traced in meat, edible tissues, milk and eggs. However due to the high concentrations of toxins involved, such findings are rare in the daily practice. In Germany today only aflatoxins (aflatoxin M1 in milk) and ochratoxin A (in blood, meat and edible tissues from swine) are of practical relevance from the view of food hygiene and food safety. Other mycotoxins at present discussed like toxins of Fusaria (trichothecenes, zearaleone, fumonisins) and ergot alkaloids are of no importance as possible contaminants in food from animal origin although they could have a negative impact on animal production.

Aflatoxins↗

PubMed1986

Effect of ethanol on the in vivo covalent binding and in vitro metabolism of aflatoxin B1 in rats.

The binding of [3H]aflatoxin B1 (AFB1) to the DNA, RNA and protein of liver after i.p. administration to rats with and without ethanol pretreatment was studied. The quantities of AFB1 binding to DNA and RNA were significantly increased by ethanol pretreatment but the formation of protein adducts was not affected. AFB1 metabolism by hepatic microsomes from ethanol-treated rats to aflatoxins M1 (AFM1) and Q1 (AFQ1) was increased when compared to those of control microsomes. These results suggest that an increase in AFB1 binding to liver nucleic acids and AFB1 metabolism after pretreatment of ethanol resulted from an increase in hepatic mixed-function oxidases and a possible decrease in hepatic glutathione (GSH) content which subsequently lead to an increase in hepatotoxicity of AFB1.

Administration, Oral↗

PubMed1975

Aflatoxin B1 hydroxylation: sensitive monooxygenase microassay suitable for liver biopsy specimens.

A method for measuring the rate of monooxygenase catalyzed hydroxylation of aflatoxin B1 to aflatoxin Q1 has been developed. It is suitable for use with small amounts of tissue obtained by needle or surgical biopsy of liver. Liver samples are homogenized in buffered saline containing a glucose-6-phosphate:NADPH generating system. 14C-AFB, is added to initiate the 10 min oxidation period. Quick-freezing stops oxidations, and AFB1 and AFQ1 are extracted using CHCl3. After solvent removal, the residue is resuspended in benzene-acetonitrile (98:2) and applied to silica gel thin-layer chromatography plates which are developed twice in chloroform-acetone-n-hexane (85:15:20). AFB1 and AFQ1 were located by fluorescence and scraped into vials for scintillation counting. The reaction was linear for 10 min using 5-10 mg liver tissue per 0.2 ml incubation. Aflatoxin M1 and 3 other metabolites more polar than AFB1 were also produced. The apparant Km for AFQ1 formation was 8.6x10(-4)M and Vmax was 287 picomoles AFQ1 mg protein-1 min-1 using bonnet monkey Macaca radiatea liver. The procedures should be valuable in comparative biochemical studies, especially those using liver biopsy specimens of primates.

Aflatoxins↗

PubMed1980

Carcinogenic response of rainbow trout (Salmo gairdneri) to aflatoxin Q1 and synergistic effect of cyclopropenoid fatty acids.

Aflatoxin Q1 (AFQ1), the major microsomal biotransformation product of aflatoxin B1 (AFB1) formed in vitro by monkey and human liver preparations, was fed to rainbow trout (Salmo gairdneri) in a semipurified diet at levels of 20 ppb for 1 year and 100 ppb for 10 months. As a test for carcinogenicity in hatched fish, it was also used at 1 ppm in a water solution and exposed for 1 hour to fertile trout eggs. The 20-ppb dietary exposure and 1-ppm egg exposure failed to elicit a carcinogenic response; however, the 100-ppb dietary exposure produced a 10.6% incidence of hepatocellular carcinomas at the end of 1 year. Administration of 50 ppm methyl sterculate, a cyclopropenoid fatty acid, in combination with 100 ppb AFQ1 resulted in a synergistic tumor response similar to that previously noted with administration of AFB1 plus aflatoxin M1. The tumor incidence was 89.1% in the fish on the combined diet. These results indicated that AFQ1 was approximately 100 times less carcinogenic than was AFB1. This comparison of carcinogenic potencies was very similar to the comparison of the relative mutagenicities of the two compounds in the Ames bacterial mutagen assay system.

Aflatoxins↗

PubMed1993

Distribution and metabolism of aflatoxin B1 in the marmoset monkey (Callithrix jacchus).

Whole-body autoradiography of [3H]aflatoxin B1 (3H-AFB1) in marmoset monkeys (Callithrix jacchus) showed a localization of bound labelling, in addition to the liver, in the nasal olfactory and respiratory mucosa and the mucosa of the nasopharyngeal duct, the pharynx, the larynx, the trachea and the oesophagus. In vitro microautoradiography of these tissues incubated with 3H-AFB1 showed a localization of bound radioactivity in some cells in the epithelial linings of the tissues. This binding was abolished when the incubations were performed in the presence of the cytochrome P-450 inhibitor metyrapone. These results indicate a cytochrome P-450-dependent bioactivation of AFB1 in some structures in the epithelia of the nasal olfactory mucosa and the upper respiratory and alimentary pathways, in addition to the liver, in the marmoset monkey. Quantitation of the in vitro formation of tissue-bound radioactivity from the 3H-AFB1 showed that the nasal olfactory mucosa had the highest capacity to form bound metabolites among the tissues examined. Liquid chromatography of lipid-soluble metabolites formed by the nasal olfactory mucosa and the liver showed that aflatoxin M1 (AFM1) was the major metabolite. AFM1 was also the major metabolite found in the liver in vivo. In the pigmented tissues of the marmosets there was an accumulation of nonmetabolized AFB1. This can be related to a melanin-affinity of AFB1. The described tissues with a capacity to accumulate and metabolize AFB1 may be potential targets for the carcinogenicity of this substance in the marmoset monkey.

Aflatoxin B1↗

PubMed1981

Aflatoxicol-induced hepatocellular carcinoma in rainbow trout (Salmo gairdneri) and the synergistic effects of cyclopropenoid fatty acids.

Aflatoxicol (AFL), a major metabolite of aflatoxin B1 (AFB1) in the Mt. Shasta rainbow trout (Salmo gairdneri), was found to produce hepatocellular carcinoma in trout. It was administered in a casein diet to duplicate groups of 120 fingering trout. In the same manner, additional duplicate groups received one of the following: no toxicant; AFB1; the diastereomer of AFL (AFL'); cyclopropenoid fatty acids (CPFA); and CPFA plus AFB1, AFL, and AFL'. Eight months after the initiation of the study, the following incidences of carcinoma were observed: control (0%); 20 ppb AFB1 (56%); 29 ppb AFL (26%); 61 ppb AFL' (0%); 50 ppm CPFA (3%); 20 ppb AFB1 plus 50 ppm CPFA (96%); 29 ppb AFL plus 50 ppm CPFA (94%); and 61 ppb AFL' plus 50 ppm CPFA (55%), showing both the carcinogenicity of AFL and the synergistic effects of CPFA. Twelve-month incidences were correspondingly higher in all cases. Aflatoxin M1, another metabolite of AFB1 in rainbow trout, was reported previously to be carcinogenic in trout. These results support the hypothesis that metabolism in rainbow trout does not effectively detoxify AFB1, but rather the formation of AFL extends the carcinogenicity of AFB1 and may contribute to the high sensitivity of rainbow trout to AFB.

Aflatoxins↗

PubMed1998

Dietary carotenoids inhibit aflatoxin B1-induced liver preneoplastic foci and DNA damage in the rat: role of the modulation of aflatoxin B1 metabolism.

To study the effects of carotenoids on the initiation of liver carcinogenesis by aflatoxin B1 (AFB1), male weanling rats were fed beta-carotene, beta-apo-8'-carotenal, canthaxanthin, astaxanthin or lycopene (300 mg/kg diet), or an excess of vitamin A (21000 RE/kg diet), or were injected i.p. with 3-methylcholanthrene (3-MC) (6 x 20 mg/kg body wt) before and during i.p. treatment with AFB1 (2 x 1 mg/kg body wt). The rats were later submitted to 2-acetylaminofluorene treatment and partial hepatectomy, and placental glutathione S-transferase-positive liver foci were detected and quantified. The in vivo effects of carotenoids or of 3-MC on AFB1-induced liver DNA damage were evaluated using different endpoints: liver DNA single-strand breaks (SSB) induced by AFB1, and in vivo binding of [3H]AFB1 to liver DNA and plasma albumin. Finally, the modulation of AFB1 metabolism by carotenoids or by 3-MC was investigated in vitro by incubating [14C]AFB1 with liver microsomes from rats that had been fed with carotenoids or treated by 3-MC, and the metabolites formed by HPLC were analyzed. In contrast to lycopene or to an excess of vitamin A, both of which had no effect, beta-carotene, beta-apo-8'carotenal, astaxanthin and canthaxanthin, as well as 3-MC, were very efficient in reducing the number and the size of liver preneoplastic foci. In a similar way as 3-MC, the P4501A-inducer carotenoids, beta-apo-8'-carotenal astaxanthin and canthaxanthin, decreased in vivo AFB1-induced DNA SSB and the binding of AFB1 to liver DNA and plasma albumin, and increased in vitro AFB1 metabolism to aflatoxin M1, a less genotoxic metabolite. It is concluded that these carotenoids exert their protective effect through the deviation of AFB1 metabolism towards detoxication pathways. In contrast, beta-carotene did not protect hepatic DNA from AFB1-induced alterations, and caused only minor changes of AFB1 metabolism: seemingly, its protective effect against the initiation of liver preneoplastic foci by AFB1 is mediated by other mechanisms.

Aflatoxin B1↗

PubMed1982

Detection of aflatoxins and related metabolites by radioimmunoassay.

Rabbit (outbred albino New Zealand White) antisera have been raised against aflatoxin B1 (AFB1) using as immunogen conjugates in which the hapten was coupled to bovine serum albumin (BSA) either through C1 or C8 with the oxime and the dichloride derivatives of AFB1 as intermediates. Radioimmunoassay (RIA), with [3H]AFB1 as tracer, showed that the antiserum prepared with the conjugate in which BSA was coupled to the AFB1 oxime derivative was highly specific to AFB1, whereas the antiserum raised against the conjugate in which BSA was coupled to AFB1 through the AFB1Cl2 derivative (C-antiserum) cross-reacted to a large extent with other aflatoxins, including aflatoxin M1, an important urinary metabolite of AFB1 in several species including humans. AFB1-related metabolites in the urine of inbred BD IV adult male rats given AFB1 orally at doses from 600 pmol to 385 nmol can easily be followed over 9 days by RIA in which the "cross-reactive" C-antiserum is used. This suggests that similar methodologies could be used for the monitoring of human exposure to AFB1.

Aflatoxin B1↗

PubMed2002

Aflatoxins in retail food products in Bursa, Turkey.

Aflatoxin B1 (AFB1) in 25 cacao hazelnut cream and 15 dried apricot samples and aflatoxin M1 (AFM1) in 130 cheese samples (35 full fatty Turkish white cheeses, 35 fresh kashars, 25 old kashars, 20 Gravyer cheeses and 15 cream cheeses) randomly collected from traditional retail markets with insufFicient chilling facilities in Bursa, Turkey, were determined by ELISA. Mean AFB1 and AFM1 in the cacao hazelnut cream, dried apricot and cheese were 1,076.5 +/- 194.4 ng/kg, 1,441.3 +/- 331.9 ng/kg and 142.2 +/- 18.7 ng/kg, respectively; 15.45% of the cheese samples exceeded the Turkish AFM1 tolerance limit of 250 ng/kg.

Aflatoxins↗

PubMedDate not supplied

Effect of dietary vitamin E (alpha-tocopherol) on aflatoxin B metabolism.

Intraperitoneal injection of rats with 2 mg/kg ring labelled 14C AFB1 (spec. act. 110 mCi/mM/nmole) showed a higher level of radioactivity in the urine of test animals on diets containing 600 mg/kg vit. E 24 h after pretreatment. Analysis of the urine by chloroform extraction, thin layer chromatography and liquid scintillation counting of the various fractions showed less aflatoxin M1 (AFM1) and less unmetabolized AFB1 in test samples than in controls. Incubation of ring labelled 14C AFB1 with hepatic 10,000 g supernatant fractions, however, showed increased metabolism of AFB1 by fractions from test animals as compared with the controls. Rate of disappearance of 14C AFB1 and the consequent formation of AFM1 was greater in the test fractions than in the controls. At 30 days all test animals showed higher levels of serum vitamin E than the controls. Hepatic aniline hydroxylase and ethyl morphine N-demethylase activities of the liver fractions and blood glutathione reductase activity were greater in the tests. P-nitroanisole-O-demethylase activity was reduced while hepatic and serum reduced glutathione levels remained basically unaltered.

Aflatoxin B1↗

PubMed1988

Comparative effect of dietary butylated hydroxyanisole and beta-naphthoflavone on aflatoxin B1 metabolism, DNA adduct formation, and carcinogenesis in rainbow trout.

Butylated hydroxyanisole (BHA) and beta-naphthoflavone (BNF), both chemicals with anti-carcinogenic properties in some experimental animals, were compared for effects on aflatoxin B1 (AFB1) metabolism, hepatic DNA adduct formation and carcinogenesis in the rainbow trout. Dietary BHA had no effect on the hepatic tumor incidence when fed at 0.03 or 0.3% 4 weeks prior to and during a 4 week dietary exposure of 10 p.p.b. AFB1. BNF, when fed at 0.005 or 0.05% under similar conditions, significantly reduced tumor response, which confirms previous results in trout (Nixon et al., Carcinogenesis, 5, 615-619, 1984). BHA fed at either 0.03 or 0.3% for 8 weeks had no post-initiation effect on the 52 week hepatic tumor incidence of trout exposed to a 0.5 p.p.m. AFB1 solution as embryos. A similar post-initiation exposure to 0.05% BNF significantly enhanced AFB1 tumor response. The influence of dietary BHA and BNF on AFB1 metabolism and DNA adduct formation and persistence in trout were examined. A 3 week pre-treatment with 0.3% dietary BHA had no effect on in vivo hepatic nuclear AFB1-DNA adduct formation at 0.5, 1, 2 and 7 days after AFB1 i.p. injection. By contrast 0.05% dietary BNF reduced hepatic AFB1-DNA adducts to 33-60% of control levels at 0.5, 1, 2 and 4 days after AFB1 exposure. This was accompanied by significantly lower blood and liver levels of AFB1 during the first 24 h after i.p. injection. Livers of BNF trout also contained 4-fold more of the less carcinogenic metabolite, aflatoxin M1, and 50% less aflatoxicol (AFL), a metabolite with similar carcinogenicity as AFB1. Bile AFL-glucuronide levels were significantly decreased in BNF-fed trout, but total bile glucuronides were significantly increased due to a 15-fold increase in aflatoxicol-M1 glucuronide. Freshly isolated hepatocytes from BHA-fed fish, when incubated with AFB1 for 1 h, showed no difference in levels of AFB1-DNA adducts or ratios of AFB1 metabolites when compared to hepatocytes isolated from fish fed a control diet only. By contrast, dietary BNF has been previously shown to greatly enhance AFM1 production, reduce AFL production, and significantly reduce AFB1-DNA adduct formation in isolated trout hepatocytes (Bailey et al., Natl. Cancer Inst. Monograph, 65, 379-385, 1984). These results indicate that dietary BHA up to 0.3% does not alter AFB1 metabolism or DNA adduction in trout, nor does it inhibit or promote AFB1 hepatocarcinogenesis in this species.(ABSTRACT TRUNCATED AT 400 WORDS)

Aflatoxin B1↗