SEARCH · PubMed Health

Results for “GLUCOSIDES”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

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

At least 217 records · Page 12Linked to original sources

PubMed1972

Mechanism of biosynthesis of thio- -D-glucuronides and thio- -D-glucosides.

1. The thio-beta-d-glucosiduronic acids (thio-beta-glucuronides) of o-aminothiophenol, diethyldithiocarbamic acid, p-nitrothiophenol and thiophenol are formed biosynthetically in broken- and intact-cell preparations of mouse liver. 2. For this biosynthesis to occur in homogenates or microsomal fractions, UDP-glucuronic acid was required during incubation; glucose, glucuronic acid or UDP could not replace it. UDP was a product of the reaction. 3. The biosynthetic mechanism linking glucuronic acid to thiol and carbodithioic groups therefore requires UDP-glucuronyltransferase activity and resembles that forming the various types of O-glucuronides. 4. An analogous enzymic mechanism employing UDP-glucose synthesizes the thio-beta-d-glucosides of diethyldithiocarbamic acid and thiophenol in gut preparations of the mollusc Arion ater; this mechanism resembles that forming the O-glucosides. The thio-beta-d-glucosides are formed also in intact cells. 5. As expected from the distribution of O-glycosides, S-glucuronides of these aglycones were not detectable with the invertebrate, nor were the S-glucosides with the vertebrate. 6. Despite their similar biosyntheses, S- and O-beta-glycosides differ in susceptibility to hydrolysis by beta-glycosidases. Rat preputial-gland beta-glucuronidase hydrolysed thioglucuronides of o-aminothiophenol, diethyldithiocarbamic acid and p-nitrothiophenol, hydrolysis being inhibited by glucarolactone; the thioglucuronide of thiophenol was not hydrolysed by preputial-gland or liver beta-glucuronidase. The two S-glucosides resisted hydrolysis by beta-glucosidase from almond emulsin.

Animals↗

PubMed1996

Specificity of binding of beta-glucoside activators of ryegrass (1-->3)-beta-glucan synthase and the synthesis of some potential photoaffinity activators.

Structure-activity relationships among glycoside activators of ryegrass (Lolium multiflorum) (1-->3)-beta-glucan synthase were investigated using a number of natural and synthetic glycosides, including some carrying photoaffinity functions. There is an absolute requirement for a beta-D-glycosyl moiety in the activator, both S- and N-glucosides are active, and the position of the glucosidic linkage in beta-glucose disaccharides has a significant effect on the affinity of binding. However, the binding requirement does not extend beyond a single beta-D-glucosyl residue, and beta-D-oligoglucosides are less effective than disaccharides. The nature of the aglycon has a major influence on the binding affinity. Hydrophobic aglycons lower the concentration required for half-maximal stimulation of the enzyme obtained from an Eadie-Hofstee plot of kinetic data (Ka) for activation, but charge aglycons increase Ka. Relative to methyl-beta-D-glucoside and cellobiose (Ka 1.1 mM), the most potent compounds tested were N-[4-(benzoyl)benzoyl]-beta-D-glucosylamine and 2'-[4-azidosalicylamino]ethyl-1-thio-beta-D-glucoside with K(a)s of approximately 30 microM. The latter also was tested for its potential to specifically label the beta-glucoside-binding site on the synthase, but under the conditions used the binding was found to be nonspecific.

Enzyme Activation↗

PubMed1975

Beta-Glucosidases from Cicer arietinum L. Purification and Properties of isoflavone-7-O-glucoside-specific beta-glucosidases.

Beta-Glucosidases specific for isoflavone 7-O-glucosides have been isolated from garbanzo plants, Cicer arietinum L. These aryl-beta-glucohydrolases occur in the different organs of the plant as multiple molecular forms. The major isoenzymes of the roots, the leaves and the hypocotyl were purified to electrophoretic homogeneity. When subjected to isoelectric focussing in polyac rylamide gels the electrophoretically homogeneous glucohydrolases were found to consist of one or two major and several minor enzymically active molecular species. In roots the beta-glucohydrolase isoenzymes constitute a considerable portion of the extractable protein, so that purification to an electrophoretically homogeneous form is easily attainable. All beta-glucosidases analyzed possess molecular weights in the range of 125 000 (ultracentrifugation) to 135 000 (Sephadex G-200) and contain two subunits of molecular weight near 68 000. The pH optimum for enzymic activity is 7--7.5 with a second optimum of 4.5--5. The isoelectric points of the various species range between pH 5.9 AND 7.1. Staining for glycoprotein was positive. Kinetic analysis demonstrated a pronounced specificity of the enzymes for aromatic substrates with glucose as the sugar moiety. alpha-Glucosides as well as disaccharides were not hydrolyzed at all. Isoflavone 7-O-glucosides are the most favoured substrates with a Km of 2 x 10(-5) M, while the Km with aromatic glucosides (i.e. salicin, 4-nitrophenyl glucoside) are 100 times larger. In addition the beta-glucosidases show a pronounced specificity for glucose in the 7-position of the flavonoid nucleus. Using isoflavone aglycones as substrates glucose transferase activity was also demonstrable. The beta-glucohydrolase activity is strongly inhibited by Hg2plus. This inhibition is partially reversible and preferentially influences the Km values of the enzymes compared to V. Agplus, glucono-1,5-lactone, ethyleneglycol monomethyl ether and glycerol are only weakly inhibitory, while glucose, p-chloromercuribenzoate and Cu2plus are without effect.

Flavonoids↗

PubMed1995

Unique cholesteryl glucosides in Helicobacter pylori: composition and structural analysis.

A chloroform-methanol-extracted lipid of Helicobacter pylori was studied. Three kinds of glycolipids, accounting for about 25% (wt/wt) of the total lipid, were detected and identified to be cholesteryl glucosides. The structures of two of them were determined to be cholesteryl-alpha-D-glucopyranoside and cholesteryl-6-O-tetrade-canoyl-alpha-D-glucopyranoside, and the plausible structure of the third one was identified as cholesteryl-6-O-phosphatidyl-alpha-D-glucopyranoside. Cholesteryl glucosides are very rare in animals and bacteria. Furthermore, those in H. pylori had an alpha-glycosidic linkage, which is rather unusual for natural glycosides, and a phosphate-linked cholesteryl glycoside like the cholesteryl-6-O-phosphatidyl-alpha-D-glucopyranoside has not been reported previously. As the cholesterol glucosides were detected in strains obtained from diverse geographical locations, the presence of cholesteryl glucosides in H. pylori is a very unique and a characteristic feature of the species. These findings add a new facet to the physiology and biochemistry, especially the cholesterol and glucose metabolism, of H. pylori. Furthermore, the cholesteryl glucosides of H. pylori showed hemolytic activities.

Cholesterol↗

PubMed2006

New iridoid glucosides from the aerial parts of Verbena brasiliensis.

Two new iridoid glucosides, verbenabraside A (1) and verbenabraside B (2), were isolated from the aerial parts of Verbena brasiliensis VELL., along with six known iridoid glucosides, gelsemiol 3-O-beta-D-glucoside (3), verbraside (4), 9-hydroxysemperoside (5), griselinoside (6), aralidioside (7), and 6alpha-hydroxyforsythide dimethyl ester (8), three known phenylethanoid glycosides, 2-phenylethyl O-beta-D-xylopyranosyl-(1-->2)-beta-D-glucopyranoside (9), acteoside (10), and leucosceptoside A (11), two known lignan glucosides, dihydroxymethyl-bis(3,5-dimethoxy-4-hydroxyphenyl) tetrahydrofuran-9 (or 9')-O-beta-glucopyranoside (12) and (+)-lyoniresinol 3alpha-O-beta-D-glucopyranoside (13), a known methyl salicylate glucoside, methyl 2-O-beta-D-glucopyranosylbenzoate (14), and two known sterols, beta-sitosterol 3-O-beta-D-glucopyranoside (15) and beta-sitosterol (16). Their chemical structures were determined on the basis of spectroscopic data. Compound 1 exhibited stronger scavenging effect on the stable free radical 1,1-diphenyl-2-picrylhydrazyl than that of alpha-tocopherol.

Iridoids↗

PubMed2002

Isolation and measurement of quercetin glucosides in flower buds of Japanese butterbur (Petasites japonicus subsp. gigantea Kitam.).

Three quercetin glucosides were isolated from flower buds of Japanese butterbur (Petasites japonicus subsp. gigantea Kitam.) together with caffeic acid as the ingredients that had DPPH radical scavenging activity, using the DPPH-HPLC method for measuring the radical scavenging activity. These quercetin glucosides were identified as quercetin 3-O-beta-D-glucoside, quercetin 3-O-beta-D-6''-O-acetylglucoside, and rutin, and the amounts of the glucosides in flower buds were also examined by HPLC. The flower buds were harvested from four different sites, the total amount of quercetin glucosides in each site was 100-170 mg/100 g fr. wt., and there were no great differences of the amounts between growing fields.

Antioxidants↗

PubMed2006

Nitric oxide inhibits, and carbon monoxide activates, islet acid alpha-glucoside hydrolase activities in parallel with glucose-stimulated insulin secretion.

We have studied the influence of nitric oxide (NO) and carbon monoxide (CO), putative messenger molecules in the brain as well as in the islets of Langerhans, on glucose-stimulated insulin secretion and on the activities of the acid alpha-glucoside hydrolases, enzymes which we previously have shown to be implicated in the insulin release process. We have shown here that exogenous NO gas inhibits, while CO gas amplifies glucose-stimulated insulin secretion in intact mouse islets concomitant with a marked inhibition (NO) and a marked activation (CO) of the activities of the lysosomal/vacuolar enzymes acid glucan-1,4-alpha-glucosidase and acid alpha-glucosidase (acid alpha-glucoside hydrolases). Furthermore, CO dose-dependently potentiated glucose-stimulated insulin secretion in the range 0.1-1000 microM. In intact islets, the heme oxygenase substrate hemin markedly amplified glucose-stimulated insulin release, an effect which was accompanied by an increased activity of the acid alpha-glucoside hydrolases. These effects were partially suppressed by the guanylate cyclase inhibitor 1H-[1,2,4]oxadiazolo-[4,3-a]quinoxalin-1-one. Hemin also inhibited inducible NO synthase (iNOS)-derived NO production probably through a direct effect of CO on the NOS enzyme. Further, exogenous CO raised the content of both cGMP and cAMP in parallel with a marked amplification of glucose-stimulated insulin release, while exogenous NO suppressed insulin release and cAMP, leaving cGMP unaffected. Emiglitate, a selective inhibitor of alpha-glucoside hydrolase activities, was able to markedly inhibit the stimulatory effect of exogenous CO on both glucose-stimulated insulin secretion and the activityof acid glucan-1,4-alpha-glucosidase and acid alpha-glucosidase, while no appreciable effect on the activities of other lysosomal enzyme activities measured was found. We propose that CO and NO, both produced in significant quantities in the islets of Langerhans, have interacting regulatory roles on glucose-stimulated insulin secretion. This regulation is, at least in part, transduced through the activity of cGMP and the lysosomal/vacuolar system and the associated acid alpha-glucoside hydrolases, but probably also through a direct effect on the cAMP system.

Animals↗

PubMed2000

Efflux of dietary flavonoid quercetin 4'-beta-glucoside across human intestinal Caco-2 cell monolayers by apical multidrug resistance-associated protein-2.

Although there is strong evidence to suggest that flavonoid consumption is beneficial to human health, the extent to which flavonoids are absorbed and the mechanisms involved are controversial. Contrary to common dogma, we previously demonstrated that quercetin 4'-beta-glucoside, the predominant form of the most abundant dietary flavonoid, quercetin, was not absorbed across Caco-2 cell monolayers. The aim of this study was to test the hypothesis that a specific efflux transporter is responsible for this lack of absorption. Transport of quercetin 4'-beta-glucoside, alone or with inhibitors, was examined with Caco-2 cell monolayers. In addition, subcellular localization of the multidrug resistance-associated proteins MRP1 and MRP2 was examined by immunofluorescent confocal microscopy. Efflux of quercetin 4'-beta-glucoside, a saturable process, was not altered by verapamil, a P-glycoprotein inhibitor, but was competitively inhibited by MK-571, an MRP inhibitor. These data in combination with immunofluorescent localization of MRP2 to the apical membrane support a role for MRP2 in the intestinal transcellular efflux of quercetin 4'-beta-glucoside. These results suggest a role for MRP2 in the transport of a new class of agents, dietary glucosides.

ATP Binding Cassette Transporter, Subfamily B↗

PubMedDate not supplied

Feeding stimulative activity of steroidal and secoiridoid glucosides and their hydrolysed derivatives toward the olive weevil (Dyscerus perforatus).

Beta-sitosteryl-D-glucoside and oleuropein isolated from the olive tree (Olea europaea) and their hydrolysed derivatives were tested by a feeding stimulative activity bioassay using the olive weevil (Dyscerus perforatus). Although the steroidal glucoside showed potent feeding stimulative activity, the activity of the aglycone (beta-sitosterol) was significantly lower than that of the glucoside. On the other hand, the difference in the activity between oleuropein, a secoiridoid glucoside, and the hydrolysed derivatives was not significant.

Animals↗

PubMed1976

[Histochemical and biochemical investigation of alpha-glucosidases by means of 2-naphthyl-alpha-D-glucoside (author's transl)].

Histochemical and biochemical studies yield the following method of choice for the in situ detection of neutral (microvillous) and acid (lysosomal) alpha-glucosidases: 12 mg 2-naphthyl-alpha-D-glucoside (dissolved in 0.5 ml N,N-dimethylformamide) and 0.6--0.8 ml hexazonium-p-rosaniline in 10 ml 0.1 M citric acid phosphate buffer for aqueous or 5 ml buffer mixed with equal parts of 2% agar for incubation with semipermeable membranes, pH 5 or 6.5. With this method neutral alpha-glucosidases can be exactly demonstrated in the brush border of the small intestine (glycoamylase, sucrase-isomaltase) and kidney of mammals, birds,fishes, amphibia and reptiles; localization of acid alpha-glucosidases is achieved at the cellular level in many organs and tissues. Fluorometric and photometric measurements prove that 2-naphthyl-alpha-D-glucoside is superior to 6-brom-2-naphthyl-alpha-D-glucoside for the demonstration of alpha-glucosidases in situ due to the lower Michaelis constant and higher maximal reaction velocity of the naphthol derivative.--Among the coupling reagents tested neutral alpha-glucosidases can be localized correctly with hexazotized p-rosaniline (with and without semipermeable membranes) for simultaneous coupling. Fast Blue B delivers false positive results in the suczedaneous and simultaneous coupling procedure using aqueous incubation media; in combination with the membrane technique azo dye can not be observed in the sections. Hexazonium-p-rosaniline inhibits neutral and acid alpha-glucosidases to nearly the same extent as Fast Blue B. Fixation of blocks of tissue in formaldehyde and glutaraldehyde suppresses alpha-glucosidases in the intestine and epididymis. The inhibition rates amount to 50 and 70% respectively. Washing in sugar solution rises enzyme activity to 65 and 50%. Species and organ dependent activity differences of neutral and acid alpha-glucosidases and changes of enzyme activity in the intestine and kidney after castration as well as in the course of pregnancy can be detected by means of biochemistry but not with the histochemical assay including minimal incubation. In comparison with p-nitrophenyl-alpha-D-glucoside the 2-naphthyl derivative is also the substrate of choice for the biochemical determination of alpha-glucosidases.--Agar gel electrophoresis reveals one band in the neutral and acid pH range.

Animals↗

PubMed2002

Potential bile acid metabolites. 24. An efficient synthesis of carboxyl-linked glucosides and their chemical properties.

A facile and efficient synthesis of the carboxyl-linked glucosides of bile acids is described. Direct esterification of unprotected bile acids with 2,3,4,6-tetra-O-benzyl-D-glucopyranose in pyridine in the presence of 2-chloro-1,3,5-trinitrobenzene as a coupling agent afforded a mixture of the alpha- and beta-anomers (ca. 1:3) of the 1-O-acyl-D-glucoside benzyl ethers of bile acids, which was separated effectively on a C18 reversed-phase chromatography column (isolated yields of alpha- and beta-anomers are 4-9% and 12-19%, respectively). Subsequent hydrogenolysis of the alpha- and beta-acyl glucoside benzyl ethers on a 10% Pd-C catalyst in acetic acid/methanol/EtOAc (1:2:2, by vol) at 35 degrees C under atmospheric pressure gave the corresponding free esters in good yields (79-89%). Chemical specificities such as facile hydrolysis and transesterification of the acyl glucosides in various solvents were also discussed.

Bile Acids and Salts↗

PubMed1985

Rhodopsin-egg phosphatidylcholine reconstitution by an octyl glucoside dilution procedure.

The transmembrane protein bovine rhodopsin was reconstituted with egg phosphatidylcholine (PC) by using a modified detergent dilution technique employing the nonionic detergent octyl-beta-D-glucoside (octyl glucoside). Using this technique, reconstituted membranes having molar phospholipid/protein ratios between 60:1 and 255:1 were prepared. This is in contrast to the results obtained when an octyl glucoside dialysis technique was employed (Jackson, M.L. and Litman, B.J. (1982) Biochemistry 21, 5601-5608). In the latter case, the highest molar phospholipid/protein ratio that could be obtained when reconstituting rhodopsin with egg PC was approximately 50:1. Reconstituted vesicles prepared by the octyl glucoside dilution technique were examined by negative stain and freeze-fracture electron microscopy, and it was found that the vesicles were unilamellar providing the molar PC/protein ratio was below about 200:1, whereas in preparations having ratios higher than this, a significant number of the vesicles were multilamellar. The mean vesicle diameter showed no trend based on the molar PC/protein ratio within the range of 82:1 to 186:1. The mean diameters of the preparations were between 520 and 850 A. Approximately equal numbers of protein particles were observed on the concave and convex fracture faces of the freeze-fracture micrographs of the reconstituted membranes which is indicative of a symmetric distribution of the protein across the bilayer.

Centrifugation, Density Gradient↗

PubMed1988

The human red cell glucose transporter in octyl glucoside. High specific activity of monomers in the presence of membrane lipids.

Human red cell membranes were stripped of peripheral proteins and partially solubilized with 50-260 mM octyl glucoside at 2-14 mg protein/ml, to find conditions that afford a high concentration of active glucose transporter after purification on DEAE-cellulose. Transporter-egg yolk phospholipid vesicles were prepared by gel filtration. The specific D-glucose equilibrium exchange activities increased with increasing dilution of the glucose transporter. At 260 mM octyl glucoside the glucose transporter became partially denaturated. At 225 mM detergent the DEAE-cellulose chromatography showed one main and one minor fraction of active glucose transporter. Nucleoside transport activity was enriched in the minor fraction. Solubilization with 75 mM octyl glucoside at 8 mg protein/ml gave a maximal concentration of purified transporter, 0.8 mg/ml, probably corresponding to complete solubilization. The phospholipids were partially retarded on the DEAE-cellulose. The specific D-glucose equilibrium exchange was high, up to 200 nmol glucose/micrograms transporter in two min at 50 mM glucose. High performance gel filtration in octyl glucoside indicated that the transporter formed dimers during the fractionation. These eluted at Mr 125,000, partially separated from the phospholipids, which appeared at Mr 55,000 (cf. Mascher, E. and Lundahl, P. (1987) J. Chromatogr. 397, 175-186). The D-glucose transport activity was low in the main fraction and high in the transporter-phospholipid fraction. Mixing of these fractions did not increase the activity. The glucose transporter is probably dependent on one or more specific membrane lipid(s). Presumably the transporter dimerizes and loses activity upon removal of these lipids.

Biological Transport↗

PubMed1987

Formation of bile acid glucosides and dolichyl phosphoglucose by microsomal glucosyltransferases in liver, kidney and intestine of man.

Formation of glucosides of the bile acids chenodeoxycholic, ursodeoxycholic, deoxycholic and hyodeoxycholic acids has been detected in microsomes from human liver, kidney and intestinal mucosa. Hepatic and extrahepatic bile acid glucosyltransferase activities were characterized with respect to kinetic parameters and other catalytic properties. Whereas no marked organ-specific differences in the affinities of individual bile acids toward hepatic and extrahepatic glucosyltransferases were observed, microsomes from extrahepatic sources showed twice to 5-times the maximal rates of bile acid glucosidation estimated with microsomes from liver. In addition to bile acid glucoside formation, microsomes from human liver, kidney and intestinal mucosa catalyzed the synthesis of dolichyl phosphoglucose acting as natural glucosyl donor in bile acid glucosidation.

Bile Acids and Salts↗

PubMed1990

Thermodynamics of the interaction of aristololactam-beta-D-glucoside with DNA. Ionic strength dependence of enthalpy and entropy.

The interaction of aristololactam-beta-D-glucoside with calf thymus DNA has been studied by measuring the changes in the absorbance of the alkaloid over a wide range of temperatures and sodium chloride concentrations. The binding parameters obtained are best fit by the neighbour exclusion model. The salt and temperature dependence of the binding constants are used to estimate the thermodynamic parameters involved in the interaction of the alkaloid with DNA. It is observed that aristololactam-beta-D-glucoside binding to DNA is an exothermic process over the entire range of salt and temperature, and the estimated values of enthalpy and entropy change are strongly dependent on the ionic strength of the solution. The enthalpy and entropy changes compensate one another to produce a relatively small Gibbs' free energy change. The possibility that aristololactam-beta-D-glucoside exists as a monovalent cation at neutral pH and the possible molecular contribution to the enthalpy and entropy changes of the aristololactam-beta-D-glucoside-DNA complex are discussed.

Alkaloids↗

PubMed1990

Castanospermine-glucosides as selective disaccharidase inhibitors.

Castanospermine (CS) is a potent but non-selective inhibitor of many glycohydrolases including the intestinal disaccharidases. Several CS-glucosides were synthesized to investigate the effect of an attached glucopyranosyl residue on the potency and selectivity of CS toward inhibition of intestinal disaccharidases. 8 alpha-glucosyl-CS and 7 alpha-glucosyl-CS were nearly as potent against sucrase activity as CS (IC50 values = 30, 40, and 20 nM respectively) but were 1/50 or less as potent as CS against lactase and trehalase activities. 8 beta-glucosyl-CS was 1/20 to 1/140 as potent as CS and 1 alpha-glucosyl-CS was 1/57 to 1/1500 as potent as CS against disaccharidase activities. 1 alpha-glc-CS was less selective than CS, whereas the other CS-glucosides were more selective. 7 alpha-glc-CS and 8 alpha-glc-CS were the most sucrase selective and were particularly ineffective against trehalase and lactase activities. 8 beta-glc-CS was similar to CS except for relatively weaker trehalase inhibition. In summary, selectivity toward certain disaccharidases was achieved by glucosylation of CS hydroxyls. However, a simple structural comparison of the CS-glucoside to a disaccharide substrate did not reliably predict which disaccharidase would be more inhibited by the CS-glucoside.

1-Deoxynojirimycin↗

PubMed1996

4-Pentafluoroethylumbelliferyl-beta-D-glucoside as a new fluorogenic substrate for acid beta-D-glucosidase.

4-Pentafluoroethylumbelliferyl-beta-D-glucoside is proposed as an efficient substrate for human leukocyte acid beta-glucosidase. Its synthesis is described. This substrate was compared directly with 4-trifluoromethylumbelliferyl-beta-D-glucoside synthesized by us earlier and with 4-methylumbelliferyl-beta-D-glucoside which is commonly used for acid beta-glucosidase activity assay. The specific activity of acid beta-glucosidase with 4-pentafluoroethylumbelliferyl-beta-D-glucoside was 3- and 8-fold higher than it was with the substrates mentioned above. The kinetic parameters KM and VMAX for human leukocyte acid beta-glucosidase with the three substrates was determined. One possible application of the newly synthesized substrate is its use in the diagnosis of acid beta-glucosidase hereditary deficiency (Gaucher's disease).

Fluorescent Dyes↗

PubMed1986

Mutagenicity of N-arylacetohydroxamic acids and their O-glucosides derived from chlorinated 4-nitrobiphenyl ethers.

The mutagenic activity of N-arylacetohydroxamic acids, their O-acetates, their O-glucosides, and N-arylhydroxylamines, derived from chlorinated 4-nitrobiphenyl ethers (CNBs), was tested in the Salmonella reversion assay. N-Arylhydroxylamines were mutagenic by themselves; however, other compounds containing an N-acetyl group showed mutagenic activity in the presence of guinea pig liver S9. The mutagenic activation of the glucosides of N-arylacetohydroxamic acids was caused by Ms but not by S10.5, whereas their aglycones, N-arylacetohydroxamic acids, were activated to mutagens by both the fractions. The mutagenic activation of these compounds was inhibited by bis(p-nitrophenyl)phosphate, which indicates that enzymatic deacetylation is a crucial step in the mutagenic activation. Analysis of metabolites of the O-glucosides of N-arylacetohydroxamic acids by h.p.l.c. indicates that the corresponding deacetylated O-glucosides are primary metabolites, which decomposed to amino and azoxy (via hydroxylamine) derivatives, and that the deacetylating activity of S9 locates exclusively in Ms.

Animals↗