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At least 955 records · Page 53Linked to original sources
PubMed1997

Arabidopsis dihydropteroate synthase: general properties and inhibition by reaction product and sulfonamides.

Dihydropteroate synthase (DHPS) (EC 2.5.1.15) was extracted from leaves of Arabidopsis thaliana and purified 21-fold by ion-exchange chromatography. This enzyme preparation was then characterized for several of its properties. Michaelis-Menten constants for the substrates, p-aminobenzoic acid and dihydropteridine diphosphate were estimated to be 2.5 and 91 microM, respectively. In an optimized assay, the reaction product, dihydropteroic acid, competitively inhibited the enzyme activity with a Ki of 81 microM. However, neither dihydropteroic acid nor tetrahydrofolate, products further downstream in the biosynthetic pathway inhibited enzymatic activity. This appears to be the first report of product inhibition of DHPS from a higher plant. The relative inhibitory properties of several sulfonamides, analogues of p-aminobenzoic acid, were also examined. The substitutions on the amide nitrogen of the sulfonamides influenced the degree of inhibition; thus I50 values for the inhibition of the DHPS activity by sulfanilamide, sulfacetamide and sulfadiazine were estimated to be 18.6, 9.6 and 4.2 microM, respectively. The competitive pattern of inhibition was shown in experiments with sulfadiazine.

Arabidopsis↗
PubMed1973

Multiple N-acetyltransferases and drug metabolism. Tissue distribution, characterization and significance of mammalian N-acetyltransferase.

Investigations in the rabbit have indicated the existence of more than one N-acetyltransferase (EC 2.3.1.5). At least two enzymes, possibly isoenzymes, were partially characterized. The enzymes differed in their tissue distribution, substrate specificity, stability and pH characteristics. One of the enzymes was primarily associated with liver and gut and catalysed the acetylation of a wide range of drugs and foreign compounds, e.g. isoniazid, p-aminobenzoic acid, sulphamethazine and sulphadiazine. The activity of this enzyme corresponded to the well-characterized polymorphic trait of isoniazid acetylation, and determined whether individuals were classified as either ;rapid' or ;slow' acetylators. Another enzyme activity found in extrahepatic tissues readily catalysed the acetylation of p-aminobenzoic acid but was much less active towards isoniazid and sulphamethazine. The activity of this enzyme remained relatively constant from individual to individual. Studies in vitro and in vivo with both ;rapid' and ;slow' acetylator rabbits revealed that, for certain substrates, extrahepatic N-acetyltransferase contributes significantly to the total acetylating capacity of the individual. The possible significance and applicability of these findings to drug metabolism and acetylation polymorphism in man is discussed.

Acetyltransferases↗
PubMedDate not supplied

Clinical and immunological responses in subjects sensitive to solvents.

Twenty patients proved sensitive to a 15-min exposure to 15 ppm toluene. We assessed patients neuropsychologically before and after toluene exposure, and they had impaired cognitive functioning characterized by a deterioration in short- and long-term memory and psychomotor coordination. We measured total immunoglobin G and T-cell antigen-binding molecules against an antigen prepared by conjugation of para-aminobenzoic acid to human serum albumin in 20 patients and 16 controls. There was no significant difference in the immunoglobulin G levels to the antigen in the 2 groups, but the levels of T-cell antigen-binding molecules against the para-aminobenzoic acid conjugated to human serum albumin were elevated significantly in subjects sensitive to toluene. We also found significant associations between T-cell antigen-binding molecule levels and (a) decreased performance on the STROOP (Colour Word) test, (b) a shift in focal length following toluene exposure, (c) clinical assessment of disability, and (d) longer histories of chemical exposure. The measurement of T-cell antigen-binding molecules against chemical haptens may be valuable in the assessment of patients who are sensitive to chemicals.

Adult↗
PubMed1992

Cloned mouse N-acetyltransferases: enzymatic properties of expressed Nat-1 and Nat-2 gene products.

N-Acetylation plays an important role in the metabolism of a wide variety of hydrazine drugs and arylamine drugs and carcinogens. Humans have genetically determined differences in their N-acetyltransferase activities and are phenotypically classified as rapid or slow acetylators. Mice have a similar genetic polymorphism in N-acetyltransferase activity and have been used as models of the human polymorphism in many studies of the toxicology and carcinogenicity of arylamines. Recently, two N-acetyltransferase genes, Nat-1 and Nat-2, were cloned from rapid (C57BL/6J) and slow (A/J) acetylator mouse strains. The genomic clone encoding NAT-1 is identical in rapid and slow acetylator mouse strains, whereas the clone encoding NAT-2 differs between rapid and slow strains by a single base pair, which changes the encoded amino acid from Asn99 in the rapid acetylator strain to Ile99 in the slow acetylator strain. In this report, the N-acetylation polymorphism in mice was investigated by transiently expressing the cloned N-acetyltransferase genes in COS-1 cells. The intronless coding regions of Nat-1 and Nat-2 showed different substrate specificities; isoniazid was a preferred substrate for NAT-1, whereas p-aminobenzoic acid was preferred for NAT-2(99asn) and NAT-2(99ile). All three enzymes acetylated 2-aminofluorene, but none of them acetylated sulfamethazine. Kinetic constants determined for the expressed enzymes with 2-aminofluorene and p-aminobenzoic acid indicated that Km values were not significantly different between the enzymes, although the Vmax value of NAT-2(99asn) was consistently 2-3-fold higher than that of NAT-1 or NAT-2(99ile). Nat-1 and Nat-2 encoded mRNAs of approximately 1.4 kilobases in livers of rapid and slow acetylators. Nat-2 mRNA was more abundant in liver than Nat-1 mRNA. The abundance of Nat-2 mRNA and Nat-1 mRNA was equivalent in both rapid and slow acetylator mouse strain livers. Incubation of transfected COS-1 cell cytosols at 37 degrees showed that the time for decline of NAT activity to 50% of its initial value was 45 hr for NAT-1, 60 hr for NAT-2(99asn), and 4 hr for NAT-2(99ile). This 15-fold difference in the heat stability of the rapid and slow isoforms of NAT activity was also observed in cytosols from rapid and slow acetylator livers. Comparison of the rates of translation of the rapid and slow isoforms of NAT-2 in an in vitro system showed that NAT-2(99asn) was translated at approximately twice the rate of NAT-2(99ile).(ABSTRACT TRUNCATED AT 400 WORDS)

Acetyltransferases↗
PubMed1988

Exocrine pancreatic function following intraoperative irradiation of the canine pancreas.

Twenty-four beagles received intraoperative irradiation (IORT) with 6 meV electrons to the pancreas and the duodenum. Intraoperative irradiation doses of 17.5 to 40 Gy were given. Billroth II gastrojejunostomy was done to bypass the irradiated duodenum. Six control dogs received only the Billroth II surgery. Two weeks postoperatively, irradiated dogs were given 50 Gy of 6 MV X radiation (external-beam radiation [EBRT]) to the pancreas and duodenum in 2 Gy fractions over a 5-week period. Dogs were monitored clinically and exocrine pancreatic function was evaluated using an N-benzoyl-l-tyrosyl-para-aminobenzoic acid (BT-PABA) test between 3 and 135 days postoperatively. Necropsies were performed on the dogs at 135 days postoperatively. The degree of gross pancreatic atrophy in the irradiated group was dose related. The mean percentage of normal acinar cells correlated with IORT doses and para-aminobenzoic acid (PABA) values (P less than 0.1). Weight loss was significantly greater in the irradiated dogs compared to the control (P less than 0.05) and the mean percentage of body weight loss correlated with the mean PABA values (P less than 0.01). In this study, the use of the BT-PABA test to evaluate progressive exocrine pancreatic function following IORT and EBRT showed an expected trend. A progressive decrease in exocrine pancreatic function in the irradiated dogs as indicated by plasma PABA levels may have been partly due to late radiation damage to acinar cells, secondary to vascular and ductular damage. At 135 days postoperatively none of the dogs showed clinical signs of exocrine pancreatic insufficiency and the plasma PABA levels were within the normal presurgical range. The progressive decrease in plasma PABA levels indicated a potential for the late development of exocrine pancreatic insufficiency. The BT-PABA test could be useful for evaluating the progressive decrease in exocrine pancreatic function and residual radiation injury to the pancreas. Because the exocrine deficiency can be managed with replacement therapy, pancreatic injury may not be a serious complication after doses of less than 30 Gy IORT with 50 Gy EBRT. Data from this study are in agreement with previous clinical and experimental reports that the duodenum is dose-limiting for IORT. Doses of 20 Gy IORT or less plus 50 Gy EBRT for treatment of carcinoma of the pancreas may not result in serious long-term complications due to radiation injury of the duodenum.

Adenocarcinoma↗
PubMed2002

Syntheses of labeled vitamers of folic acid to be used as internal standards in stable isotope dilution assays.

[2H4]Folic acid was synthesized by deuterating p-aminobenzoic acid, which was then coupled to glutamic acid and 6-formylpterin. Using [2H4]folic acid as starting component enabled the preparation of labeled vitamers tetrahydrofolate, 5-formyltetrahydrofolate, 5-methyltetrahydrofolate, and 10-formylfolate which were characterized by electrospray mass spectrometry and collision-induced dissociation. The mass spectrometric studies confirmed that the compounds could be used as internal standards in stable isotope dilution assays.

4-Aminobenzoic Acid↗
PubMed1993

Sequence and mapping of the aroA gene of Staphylococcus aureus 8325-4.

The aroA gene of Staphylococcus aureus 8325-4 was cloned. Sequence analysis and the phenotype of directed plasmid insertions 5' to aroA suggest that aroA is located in an operon and that it maps 3' to the aroC and aroB genes. A revised consensus sequence for the aroA gene product EPSP synthase binding site for its substrate (phosphoenolpyruvate) and an inhibitor (glyphosate) is proposed. An aroA insertion mutant isolated by allelic replacement was employed in genetic mapping experiments which demonstrated the gene order thy aroA tyrB in SmaI fragment A of the S. aureus 8325-4 chromosome. The aroA::Tcr mutant required aromatic amino acids but remained independent of p-aminobenzoic acid (PAB). This could be due to the insertion being located close to the 5' end of the gene, allowing expression of a truncated protein. The PAB independence may explain the finding that the mutant was not attenuated in mouse infection experiments. It was not possible to isolate a null mutant in aroA.

3-Phosphoshikimate 1-Carboxyvinyltransferase↗
PubMed1980

Evaluation of antifibrotic drugs in bleomycin-induced pulmonary fibrosis in hamsters.

Endotracheal administration of bleomycin to hamsters causes severe pulmonary fibrosis. We have examined the utility of this response as a model for the screening of pulmonary antifibrotic agents. The time course of collagen synthesis after bleomycin administration was examined in neutral salt soluble and insoluble fractions by in vitro incubation of minced lung with [14C] proline. Collagen synthesis increased to approximately 250% above control in both neutral salt soluble and insoluble collagen fractions by day 6 after bleomycin. Noncollagenous protein synthesis was also increased but to a lesser amount. The early rise in collagen synthesis leads to accumulation of collagen that can be biochemically quantitated within 1 week. This time course is advantageous for short-term testing of antifibrotic agents. In the present study, beta-aminopropionitrile, D-penicillamine, and p-aminobenzoic acid were examined. All three agents were found to reduce significantly the accumulation of neutral salt insoluble collagen in bleomycin-treated animals.

4-Aminobenzoic Acid↗
PubMed1980

The hairless mouse as a model for evaluating sunscreens. Prevention of ultraviolet B inhibition of epidermal DNA synthesis.

A sunscreen's effectiveness is usually determined by its ability to prevent ultraviolet (UV) radiation-induced skin erythema. This criterion requires subjective interpretation. We propose a new method of evaluating sunscreens based on the known effect of UV-B radiation (290 to 320 nm) to inhibit DNA synthesis. Using hairless mice, we found that sulisobenzone (Uval) and aminobenzoic acid (PreSun) sunscreens differ substantially in their ability to prevent inhibition of epidermal cell DNA synthesis by UV-B radiation. By estimating the UV-B dose required to inhibit DNA synthesis by 50%, with and without sunscreen, a protective factor of 5.6 and 14.4 was calculated for sulisobenzone and aminobenzoic acid, respectively. This technique is an objective way to evaluate sunscreen effectiveness and could be a useful screening procedure for sunscreen preparations before final efficacy testing in humans.

Animals↗
PubMedDate not supplied

[Biosynthesis of folic acid in Eimeria tenella (Coccidia)].

The inhibitory analysis has shown that E. tenella does not include ready folic acid into metabolic process but synthesizes its metabolite, 7:8-dihydrofolic acid (DHFA), from its precursor, para-aminobenzoic acid (PABA), which enters the host's organism. PABA can be fully substituted in the process of metabolism by sulphadimesin (SD) at the molar ratio PABA: SD=1: 16.7. As a concurrent antagonist of PABA SD is 6 times stronger in the parasite-host system of Coccidia than in bacteria in cultural medium. The increase in PABA content in relation to SD more than 1: 16.7 intensifies the viability of Coccidia that is expressed in higher lethality of chicks, which reaches its maximum at PABA : SD=1 : 1.25. A further increase in the content of PABA does not affect the host's lethality. The decrease in PABA in relation to SD lower than 1 : 16.7 reduces the viability of Coccidia. Nucleic bases G, A transforming in the organism into corresponding nucleotids and aminoacids, 1-metionin and glycine, which are the products of biosynthesis with a participation of DHFA, do not stimulate the viability of E. tenella that apparently is associated with the non-capability of the host to assimilate timidin.

4-Aminobenzoic Acid↗
PubMed1986

Exocrine pancreatic function as determined in a same-day test with use of bentiromide and p-aminosalicylic acid.

We describe a new approach to the bentiromide test of exocrine pancreatic function, p-Aminosalicylic acid (PAS), a compound closely related to the bentiromide fragment p-aminobenzoic acid (PABA), is used as a marker of the pharmacokinetic behavior of PABA to derive a PABA excretion index. This index is identical to that derived with [14C]-PABA. Concentrations of both PABA and PAS are measured in urine by "high-performance" liquid chromatography, which avoids the drug interferences encountered with established assays of PABA. We discuss the practical and diagnostic advantages of this new approach to the bentiromide test.

4-Aminobenzoic Acid↗
PubMed1991

Molecular and genetic analyses of arylamine N-acetyltransferase polymorphism of rabbit liver.

A cDNA clone encoding the full coding region of polymorphic arylamine N-acetyltransferase was isolated from rabbit liver and expressed in Chinese hamster ovary cells. The expressed enzyme acetylated 2-aminofluorene, procainamide, sulfamethazine, and p-aminobenzoic acid at equivalent rates. N-Acetyltransferase activity was measured in 17 rabbits from an inbred colony which were classified into rapid, intermediate, and slow acetylators. The livers of the rapid and intermediate acetylators efficiently acetylated all four substrates, while the liver from the slow acetylator showed a low but significant activity with p-aminobenzoic acid. Immunoblot and Northern blot analyses of rabbit livers indicated that the differences in N-acetyltransferase activity were due to differences in N-acetyltransferase protein and mRNA content. Genomic clones of N-acetyltransferase were isolated from the rapid and slow acetylator rabbits. The nucleotide sequence of the gene from rapid acetylator rabbit was identical to that of the cDNA, while the sequence of the gene from slow acetylator rabbit was homologous, but not identical, to the cDNA sequence. Genomic Southern blot and polymerase chain reaction analyses of the genomic DNAs and cDNAs from the three types of acetylator indicated that the gene for polymorphic arylamine N-acetyltransferase is totally deleted in the slow acetylator rabbit, while the gene from slow acetylator rabbit is expressed in all rabbits and might encode another N-acetyltransferase. Thus the genetic mechanism of N-acetyltransferase polymorphism in rabbit liver is essentially different from that of human liver as demonstrated in this laboratory (Ohsako, S., and Deguchi, T. (1990) J. Biol. Chem. 265, 4630-4634; Deguchi, T., Mashimo, M., and Suzuki, T. (1990) J. Biol. Chem. 265, 12757-12760).

Amino Acid Sequence↗
PubMed1982

Activation volumes for horseradish peroxidase compound II reactions.

The activation volumes for the reactions of horseradish peroxidase compound II with L-tyrosine, 3-iodo-L-tyrosine, p-aminobenzoic acid and ferrocyanide were determined by using a high-pressure stopped-flow technique at 25 degrees C and pH 7. For the tyrosines, the solvent electrostriction accompanying substrate ionization and H+ transfer from the substituted phenol to a basic group of the enzyme can account for the observed negative activation volumes. For p-aminobenzoic acid a simple electron transfer without H+ transfer appears to occur. The positive activation volume for ferrocyanide may be explained in terms of electron transfer associated with a large change in electrostriction of the inorganic redox couple.

Enzyme Activation↗
PubMed1978

Reductive drug metabolism in isolated perfused rat liver under restricted oxygen supply.

1. Hepatic azo and nitro reductase activities were studied in the perfused rat liver under normal and restricted oxygen supply. 2. Formation of sulphanilamide or p-aminobenzoic acid from neoprontosil or p-nitrobenzoic acid under aerobic conditions of liver perfusion was negligible, even at a reduced oxygen saturation of a pO2 of 300 mm Hg in the haemoglobinfree perfusion system. At a pO2 of 200 mm Hg reductase activities were almost maximal. 3. Conjugation of sulphanilamide (0-08 mM) was similar under aerobic and anaerobic conditions. Hepatic elimination of p-aminobenzoic acid (0-08 mM) showed an oxygen-dependent increase for 15 min after addition of substrate. 4. p-Nitroanisole demethylation was inhibited 80% under hypoxic perfusion at 200 mm Hg pO2 and was completely inhibited after gassing with anoxic mixtures. 5. Restitution of aerobic conditions after 30 min anaerobic perfusion restored hepatic respiration, lactate pyruvate ratio, and pH value to levels found under aerobic conditions, but bile flow remained 50% reduced.

Animals↗
PubMed1986

N-acetyltransferase multiplicity and the bioactivation of N-arylhydroxamic acids by hamster hepatic and intestinal enzymes.

The mechanism-based inactivation (suicide inactivation) by N-hydroxyphenacetin (NHP) of N-arylhydroxamic acid N,O-acyltransferase (AHAT) and p-aminobenzoic acid N-acetyltransferase (PABA NAT) activities of a partially purified hamster liver preparation was investigated. The inactivation of both enzyme activities was irreversible, but a partial protection of PABA NAT could be achieved by inclusion of the nucleophile cysteine in the incubation mixture; cysteine did not reduce the extent of inactivation of AHAT by NHP. Hepatic AHAT and PABA NAT activities were separated by affinity chromatography, and the resolved enzyme activities were subjected to incubation in the presence of NHP, N-hydroxy-2-acetamidofluorene (N-OH-AAF), and N-hydroxy-4-acetamidobiphenyl (N-OH-AABP); AHAT, but not PABA NAT, was inactivated by NHP, N-OH-AAF and N-OH-AABP. Incubation of hamster heptic PABA NAT with radiolabeled N-OH-AAF resulted in the formation of only 15% as much fluorenylamine-tRNA adduct as was formed when N-OH-AAF was bioactivated with hamster hepatic AHAT. Hamster intestinal AHAT and PABA NAT activities also were resolved by affinity chromatography; the intestinal AHAT fractions were much more effective than the PABA NAT fractions in bioactivating N-OH-AAF. These results demonstrate that hamster liver and intestine contain at least two arylamine transacetylating activities, one of which is much more effective than the other in the bioactivation of toxic and carcinogenic N-arylhydroxamic acids.

2-Acetylaminofluorene↗
PubMedDate not supplied

Genetic control of acetyl coenzyme A-dependent arylamine N-acetyltransferase, hydrazine N-acetyltransferase, and N-hydroxy-arylamine O-acetyltransferase enzymes in C57BL/6J, A/J, AC57F1, and the rapid and slow acetylator A.B6 and B6.A congenic inbred mouse.

Acetyl coenzyme A-dependent N-acetyltransferase and O-acetyltransferase activities were examined in liver cytosols derived from homozygous rapid acetylator C57BL/6J and A.B6 congenic inbred mouse strains, from homozygous slow acetylator A/J and B6.A congenic inbred mouse strains, and from the (C57BL/6J x A/J)F1 heterozygous acetylator hybrid mouse strain. Acetylator genotype-dependent N-acetyltransferase activity was exhibited for the N-acetylation of p-aminobenzoic acid, 2-aminofluorene, and 4-aminobiphenyl. In contrast, levels of isoniazid N-acetyltransferase and N-hydroxy-3,2'-dimethyl-4-aminobiphenyl O-acetyltransferase activities in mouse liver cytosol appeared to be independent of the arylamine Nat acetylator gene. Although cytosolic N-acetyltransferase activities differed about 2-fold between the parental C57BL/6J and A/J strains for p-aminobenzoic acid, 2-aminofluorene, and 4-aminobiphenyl, the same N-acetyltransferase activities differed about 6-7-fold between the homozygous rapid acetylator A.B6 and the homozygous slow acetylator B6.A congenic inbred strains. Partial purification of acetyl coenzyme A-dependent arylamine N-acetyltransferase activity in the five inbred mouse strains showed one major paraoxon-resistant enzyme in liver cytosol in each of the rapid and slow acetylator mouse strains examined. Levels of partially purified 2-aminofluorene and 4-aminobiphenyl N-acetyltransferase activity were about 7-fold higher in the A.B6 than the B6.A congenic inbred strain. Partial purification of acetyl coenzyme A-dependent isoniazid N-acetyltransferase activity showed catalysis by a paraoxon-resistant enzyme(s) distinct from the major arylamine N-acetyltransferase enzyme(s). These results suggest that isoniazid N-acetyltransferase(s) in mouse liver cytosol is a product of a separate gene that segregates independently of the arylamine Nat gene.(ABSTRACT TRUNCATED AT 250 WORDS)

Acetyl-CoA C-Acetyltransferase↗
PubMed1999

Arylamine N-acetyltransferase: a possible promoter in Helicobacter pylori-related gastric carcinogenesis.

BACKGROUND: The hypothesis of an association between peptic ulcer and infection by Helicobacter pylori in the gastroduodenal tract was suggested by Marshall and Warren in 1984. H pylori infection of the stomach is the most frequent infection in the world and exhibits an age-dependent increase. However, only a very small percentage of those infected develop gastric carcinoma, suggesting that H pylori acts as a cofactor in the pathogenesis of gastric carcinoma. N-Acetyltransferase (NAT) is expressed in uroepithelial cells and colon cytosol, while cytosolic acetyltransferase plays a critical role in susceptibility to arylamine-induced bladder and colon cancer. The presence of NAT activity in H pylori has yet to be determined. METHODS: NAT activity in H pylori from patients with peptic ulcer was studied using an acetyl coenzyme A (AcCoA) recycling assay and high-pressure liquid chromatography with p-aminobenzoic acid and aminofluorene substrates. RESULTS: The NAT activities from a number of H pylori samples were found to be 0.68 +/- 0.10 nmol/min/10(10) colony-forming units (CFUs) (intact bacteria); and 0.90 +/- 0.22 nmol/min/mg protein (cytosol) for the acetylation of 2-aminofluorene, and 0.63 +/- 0.06 nmol/min/10(10) CFUs (intact bacteria) and 0.72 +/- 0.24 nmol/min/mg protein (cytosol) for the acetylation of p-aminobenzoic acid. CONCLUSIONS: These studies show that H pylori has NAT activity, from which we speculate that the bioactivation of food-borne heterocyclic aromatic amines into genotoxic and carcinogenic products in the stomach is a possible promoter in the pathogenesis of gastric cancer.

Acetylation↗
PubMedDate not supplied

Arylamine N-acetyltransferase activity and 2 aminofluorene-DNA adducts formation in rat glial tumor cells.

Arylamine N-acetylation capacity by the N-acetyltransferase (NAT) may be an important causative factor in the initiation of cancer. Arylamine-DNA adducts formation have been correlated with the carcinogenic effect of heterocyclic aromatic amines. NAT activity in rat glial tumor cells was measured by high performance liquid chromatography (HPLC) using 2-aminofluorene (2-AF) and p-aminobenzoic acid (PABA) as substrares. 2-AF-DNA adducts formation in rat glial tumor cells was investigated by gamma-[32p]-dATP and HPLC using 2-aminofluorene as substrates. The activities (Mean +/- SD) of NAT in rat glial cells was 1.08 +/- 0.18 nmol/min/mg protein for the acetylation of 2-aminofluorene (n = 12), and 0.96 +/- 0.16 nmol/min/mg protein for the acetylation of p-aminobenzoic acid (n = 12). 2-AF-DNA adducts formation in rat glial tumor cells with 30 microM and 60 microM AF were 0.48 +/- 0.16 and 0.70 +/- 0.12 pmol/mg DNA, respectively. The results indicate that NAT was present in rat glial tumor cells, activating AF to become a metabolite able to bind covalently with DNA to form 2-AF-DNA.

Animals↗