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At least 19 recordsLinked to original sources
PubMed1976

Quantitative determination of benzyl benzoate in benzyl benzoate lotion NF.

The development of a simple, shorter and more accurate method than the NF method for the determination of benzyl benzoate in Benzyl Benzoate Lotion NF is discussed. Hydrolyzed benzyl benzoate was measured spectrophotometrically. Interference from other ingredients of the lotion, oleic acid and triethanolamine was almost negligible. The proposed method was completed in approximately 15 minutes, as opposed to the two hours required by the NF procedure.

Benzoates↗
PubMed1979

Effect of hydroxyl group substituents on pyran ring on hydrolysis rate of benzoates: 2-tetrahydropyranyl benzoate.

The hydrolysis of 2-tetrahydropyranyl benzoate was followed spectrophotometrically at 240 nm and was first order with respect to the compound, independent of pH, and very sensitivie to solvent polarity and had an isotope effect (kD2O/kH2O) near unity. The pH-independent hydrolysis rate was about 1 X 10(6) times faster than that of the corresponding glucosly benzoate. The results suggest that the presence of hydroxyl groups on the pyran ring has tremendous effect on the hydrolysis rate of these compounds.

Benzoates↗
PubMed1979

Induction of sexual receptivity by oestradiol benzoate in cyclic female rats: influence of ovarian secretions before injection of oestradiol benzoate.

The ability of cyclic female rats to show sexual receptivity 24 h after an injection of 2 microgram oestradiol benzoate (OB) was lost 24 h after ovariectomy. Exposure of cyclic rats to antioestrogen (nitromophene monocitrate) implants 24 h before ovariectomy and OB treatment prevented the latter from inducing sexual receptivity within 24 h of administration. Treatment of ovariectomized rats with constant release implants filled with an oil solution of 15 microgram oestradiol/ml had no behavioural effect in itself, but prepared the rats to show lordosis 24 h after administration of OB. Progesterone treatment (4 mg) induced sexual behaviour in cyclic rats on days other than that of the oestrous cycle when the rats are normally receptive. Evidence is presented that a lower level of oestradiol stimulation than that present duing pro-oestrus was needed for the induction of sexual receptivity in ovariectomized rats. It is suggested that the low basal level of oestradiol which was present throughout the oestrous cycle was necessary for the induction of sexual receptivity and that an increase in oestradial stimulation served to increase the behavioural sensitivity to progesterone.

Animals↗
PubMed1975

[Pharmacological study of 9 alpha-fluoro-11 beta, 17, 21-trihydroxy-16 beta-methylpregna-1, 4-diene-3,20-dione-17-benzoate (betamethasone-17-benzoate, MS-1112), a local anti-inflammatory agent. (1). Its anti-inflammatory and other pharmacological properties].

The anti-inflammatory activity and the other pharmacological properties of MS-1112, a new steroid compound, were examined and compared with other glucocorticoid analogues such as hydrocortisone acetate (Hydr), betamethasone 17-valerate (Val) and dexamethasone (Dexa). Systemically administered MS-1112 and glucocorticoids had a significant effect in inhibiting rat paw edema induced by various phlogistic stimulations and increasing vascular permeabilities and granuloma formation by cotton pellet or granuloma pouch. The order of those inhibiting activity was, in general, Dexa greater than MS-1112 greater than Val greater than Hydr. Concomitantly, Xthymolysis and adrenal weight suppression and reduced rate of body weight gain after multiple systemical administration were also observed. Locally administered MS-1112 caused an inhibiting activity, without systemic side-effects. This activity was approximately 3 to 5 times more potent than that of Dexa in rat carrageenin paw edema and cotton pellet granuloma. MS-1112 was less active than Dexa in glycogen liver deposition activity and in the depression of plasma level of corticosterone but more active than Val and Hydr. In the dose administered, MS-1112 had neither androgenic and anabolic nor estrogenic and anti-estrogenic activity. From this data, it concluded that MS-1112 is a very potent agent applicable regarding permeability and retention of steroids in a local site.

Administration, Topical↗
PubMed1975

[Pharmacological study on 9 alpha-fluoro-11 beta, 17,21-trihydroxy-16 beta-methyl pregna-1, 4-diene-3,20-dione-17-benzoate(betamethasone-17-benzoate, MS-1112), a local anti-inflammatory agent. (2). Its action of delayed hypersensitivity dermatitis].

The anti-inflammatory activity of MS-1112, a new steroid compound, after topical application and systemical administration was examined by means of delayed-type hypersensitivity in mice and compared with other glucocorticoid analogues, betamethasone-17-valerate (Val), dexamethasone (Dexa) and betamethasone (Beta). In the case of pretreatment and therapeutic effect, topically applied MS-1112 was most active in inhibiting the delayed-type hypersensitivity induced by picryl chloride. The order of those inhibitory activities of MS-1112 and Val was ointment greater than cream greater than gel. In contrast to MS-1112 and Val, inhibitory action of Dexa was slow in onset after the topical application. It appears that esterification of the 17-hydroxyl group increases the anti-inflammatory activity after topical application. While systemically administered, MS-1112 was more potent than Val, and similarly potent to Beta, but less active than Dexa. From the above results, it may be considered that topically applied MS-1112 is superior to other glucocorticoids in the percutaneous penetration and retention in the skin. MS-1112 is thus considered to be a very potent agent as a dermatocorticoid.

Administration, Topical↗
PubMed1976

Anaerobic degradation of benzoate to methane by a microbial consortium.

A stabilized consortium of microbes which anaerobically degraded benzoate and produced CH4 was established by inoculation of a benzoate-mineral salts medium with sewage sludge; the consortium was routinely subcultured anaerobically in this medium for 3 years. Acetate, formate, H2 and CO2 were identified as intermediates in the overall conversion of benzoate to CH4 by the culture. Radioactivity was equally divided between the CH4 and CO2 from the degradation of uniformly ring-labeled [14C]benzoate. The methyl group of acetate was stoichiometrically converted to CH4. Acetate, cyclohexanecarboxylate, 2-hydroxycyclohexanecarboxylate, o-hydroxybenzoic acid and pimelic acid were converted to CH4 without a lag suggesting that benzoate was degraded by a reductive pathway. Addition of o-chlorobenzoate inhibited benzoate degradation but not acetate degradation or methane formation. Two methanogenic organisms were isolated from the mixed culture; neither organism was able to degrade benzoate, showing that the methanogenic bacteria served as terminal organisms of a metabolic food chain composed of several organisms. Removal of intermediates by the methanogenic bacteria provided thermodynamically favorable conditions for benzoate degradation.

Acetates↗
PubMed1975

Purification, properties and induction of a specific benzoate-4-hydroxylase from Aspergillus niger (UBC 814).

An inducible benzoate-4-hydroxylase has been partially purified from crude extracts of the mycelial felts of Aspergillus niger. This enzyme catalyzes the transformation of benzoate to p-hydroxybenzoate with equimolar consumption of NADPH and O2. It requires tetrahydropteridine as a prosthetic group. The optimum activity was found at pH 6.2 with a Km value at 30 degrees C of 1.6-10-minus 4 for NADPH and 1.3-10-minus 4 M for benzoate. Fe-2+ (iron) is required for the enzyme activity. The enzyme is stabilized by the inclusion of benzoate, EDTA and glutathione in the extracting buffer. The enzyme is specific for benzoate as substrate. Sulfhydryl groups(s) are essential for enzyme activity as indicated by p-chloromercuri-benzoate and N-ethylmaleimide inactivation. Benzoate-4-hydroxylase activity is decreased in the mycelial felts of Aspergillus niger grown in the presence of higher concentrations of benzoate. Maximum activity of the enzyme was observed at 36 h after inoculation.

Aspergillus↗
PubMed1992

Clinical significance of benzoate-metabolizing capacity in patients with chronic liver disease: pharmacokinetic analysis.

Benzoate-metabolizing capacity was studied in control subjects and in liver disease patients after intra-venous loading of 15 mg benzoate per kg of body weight. In the 7 control subjects, the mean level (+/- SEM) of Cmax for serum benzoate was 104.1 +/- 6.8 micrograms/ml, AUC was 2.57 +/- 0.32 mg.min/ml, MRT was 21.5 +/- 1.5 min and T1/2 was 15.5 +/- 1.3 min. For serum hippurate, on the other hand, Tmax was 27.9 +/- 6.0 min, Cmax was 33.4 +/- 2.1 micrograms/ml, AUC was 1.96 +/- 0.13 mg.min/ml, MRT was 39.6 +/- 2.9 min and T1/2 was 30.7 +/- 2.4 min. In 12 patients with chronic hepatitis, Cmax, AUC, MRT and T1/2 for benzoate and Tmax, MRT and T1/2 for hippurate remained at control levels, but Cmax and AUC for hippurate were slightly decreased compared to controls. However, in 18 patients with liver cirrhosis, Cmax and AUC for benzoate were in the control range but MRT and T1/2 were significantly delayed (p less than 0.01 for both). Moreover, the MRT value was increased in proportion to the severity of liver disease (p less than 0.01). AUC for hippurate was not changed to any extent, and Tmax, MRT and T1/2 were slightly delayed, while Cmax was significantly reduced. AUC, MRT and T1/2 for benzoate and Tmax, MRT and T1/2 for hippurate showed significant correlation with serum albumin levels, prothrombin time and indocyanine green clearance rate. These results suggest that benzoate-metabolizing capacity, especially as indicated by the MRT value for serum benzoate, appears to be a better index than the indocyanine green clearance rate for determining hepatic functional reserve in chronic liver disease.

Adult↗
PubMed1975

The metabolism of benzoate by Moraxella species through anaerobic nitrate respiration. Evidence for a reductive pathway.

Moraxella sp. isolated from soil grows anaerobically on benzoate by nitrate respiration; nitrate or nitrite are obligatory electron acceptors, being reduced to molecular N2 during the catabolism of the substrate. This bacterium also grows aerobically on benzoate. 2. Aerobically, benzoate is metabolized by ortho cleavage of catechol followed by the beta-oxoadipate pathway. 3. Cells of Moraxella grown anaerobically on benzoate are devoid of ortho and meta cleavage enzymes; cyclohexanecarboxylate and 2-hydroxycyclohexanecarboxylate were detected in the anaerobic culture fluid. 4. [ring-U-14C]Benzoate, incubated anaerobically with cells in nitrate-phosphate buffer, gave rise to labelled 2-hydroxycyclohexanecarboxylate and adipate. When [carboxy-14C]benzoate was used, 2-hydroxycyclohexanecarboxylate was radioactive but the adipate was not labelled. A decarboxylation reaction intervenes at some stage between these two metabolites. 5. The anaerobic metabolism of benzoate by Moraxella sp. through nitrate respiration takes place by the reductive pathway (Dutton & Evans, 1969). Hydrogenation of the aromatic ring probably occurs via cyclohexa-2,5-dienecarboxylate and cyclohex-1-enecarboxylate to give cyclohexanecarboxylate. The biochemistry of this reductive process remains unclear. 6. CoA thiol esterification of cyclohexanecarboxylate followed by beta-oxidation via the unsaturated and hydroxy esters, would afford 2-oxocyclohexanecarboxylate. Subsequent events in the Moraxella culture differ from those occurring with Rhodopseudomonas palustris; decarboxylation precedes hydrolytic cleavage of the alicyclic ring to produce adipate in the former, whereas in the latter the keto ester undergoes direct hydrolytic fission to pimelate.

Anaerobiosis↗
PubMed1976

Characterization of a benzoate permease mutant of Pseudomonas putida.

A spontaneous mutant of Pseudomonas putida (PRS 2017) has been isolated which is incapable of growth on benzoate, does not induce the enzymes of the catechol branch of the beta-ketoadipate pathway when grown in the presence of benzoate, cannot accumulate radioactively labeled benzoate, yet grows well with mandelate as sole source of carbon and energy. This strain apparently lacks a benzoate permease, which in the wild type shows a Km of about 0.1 mM for benzoate, is inducible, and is not under the control of the regulatory system which governs the induction of the enzymes of the catechol branch of the beta-ketoadapate pathway. The lesion in PRS2017 is apparently single site and maps near other genes governing benzoate dissimilation.

Adipates↗
PubMed1978

Kinetics of biodegradation of p-nitrobenzoate and inhibition by benzoate in a pseudomonad.

The degradation of p-nitrobenzoate (p-NBA) by domestic sewage was inhibited by benzoate, and a model for this behavior was found in a soil isolate. The isolate, a pseudomonad, utilized p-NBA and benzoate by separate adaptive enzyme pathways. In oxygen uptake experiments, the degradation of p-NBA was competitively inhibited by benzoate, but the degradation of benzoate was not affected by the presence of p-NBA. 4-Nitrocatechol was not implicated in the inhibition. p-Hydroxybenzoate, which is the p-NBA degradation pathway, also had a decreased rate od degradation when benzoate was present. The growth rate of the isolate on the aromatic substrates and on glucose autoclaved in the medium was 0.3 h-1. When glucose was autoclaved separately, the growth rate was less, about 0.2 h-1. The apparent Km in oxygen uptake experiments was 25 micrometer for p-NBA and benzoate and 5 micrometer for p-hydroxybenzoate.

Benzoates↗
PubMed1976

Percutaneous absorption of betamethasone 17-benzoate measured by radioimmunoassay.

Percutaneous absorption was studied in patients following topical application of betametahsone 17-benzoate cream and gel with occlusion by means of a sensitive and specific radioimmunoassay method. Concentrations of betamethasone 17-benzoate in plasma were between 0.3 and 5 ng/ml, indicating approximately 0.05 to 0.3% of the steroid applied to the skin was detected in plasma. Plasma betamethasone 17-benzoate levels increased in proportion to the amount of the steroid applied to the skin. High correlation between plasma betamethasone 17-benzoate levels and percent inhibition of plasma cortisol was also observed. Approximately 3 ng/ml levels of betamethasone 17-benzoate in plasma induced 90% inhibition of plasma cortisol. The data suggest that betamethasone 17-benzoate in gel base was more readily absorbed than in cream base.

Administration, Topical↗
PubMed1990

Effect of fluorinated analogues of phenol and hydroxybenzoates on the anaerobic transformation of phenol to benzoate.

The effects of fluorinated analogues on the anaerobic transformation of phenol to benzoate were examined. At greater than or equal to 250 microM 2- or 3-fluorophenol, phenol transformation was delayed. 2-Fluorophenol had no apparent effect on subsequent degradation of benzoate, but benzoate accumulated in the presence of greater than or equal to 250 microM 3-fluorophenol. In contrast, 4-fluorophenol at less than or equal to 2 mM had no effect on either phenol transformation or benzoate degradation. Phenol and 2-, or 3-fluorophenol were transformed simultaneously, but phenol was transformed more rapidly than either fluorophenol. Thus, fluorinated analogues of phenol did not prevent anaerobic transformation of phenol to benzoate. 2-Fluorophenol was converted to 3-fluorobenzoate, and phenol enhanced the rate and extent of its transformation. 3-Fluorophenol was transformed to 2-fluorobenzoate to a limited extent (approximately 3%) when phenol was present. 4-Fluorophenol was not transformed regardless of the presence of phenol. 3-Fluoro-4-hydroxybenzoate, a potential fluorinated intermediate product of para-carboxylation, was transformed rapidly to 2-fluorophenol and 3-fluorobenzoate, irrespective of the presence of phenol, indicating that both dehydroxylation and decarboxylation occurred. Initially, 2-fluorophenol and 3-fluorobenzoate were rapidly formed in an approximate molar ratio of 2:1. Once 3-fluoro-4-hydroxybenzoate was completely removed, the 2-fluorophenol, initially formed, was converted to 3-fluorobenzoate at a slower rate. Thus, phenol enhanced transformation of the fluorinated analogues, and the products of transformation suggested para-carboxylation. 3-Fluoro-2-hydroxybenzoate was not transformed in either the presence or absence of phenol, indicating that ortho-carboxylation did not occur.

Anaerobiosis↗
PubMed1992

Purification and characterization of benzoyl-CoA ligase from a syntrophic, benzoate-degrading, anaerobic mixed culture.

The benzoyl-CoA ligase from an anaerobic syntrophic culture was purified to homogeneity. It had a molecular mass of around 420 kDa and consisted of seven or eight subunits of 58 kDa. The temperature optimum was 37-40 degrees C, the optimum pH around 8.0 and optimal activity required 50-100 mM TRIS-HCl buffer, pH 8.0 and 3-7 mM MgCl2; MgCl2 in excess of 10 mM was inhibitory. The activation energy for benzoate was 11.3 kcal/mol. Although growth occurred only with benzoate as a carbon source, the benzoyl-coenzyme A (CoA) ligase formed benzoyl-CoA esters with benzoate, 2-, 3- and 4-fluorobenzoate, picolinate, nicotinate and isonicotinate. Acetate was activated to acetyl-CoA by an acetyl-CoA synthetase. The Km values for benzoate, 2-, 3- and 4-fluorobenzoate were 0.04, 0.28, 1.48 and 0.32 mM, the Vmax values 1.05, 1.0, 0.7 and 0.98 units (U)/mg, respectively. For reduced CoA (CoA-SH) a Km of 0.07 mM and a Vmax of 1.05 U/mg and for ATP a Km of 0.16 mM and a Vmax of 1.08 U/mg was determined. Benzoate activation was inhibited by more than 6 mM ATP, presumably by pyrophosphate generation from ATP. The inhibition constant (Ki) for pyrophosphate was 5.7 mM. No homology of the N-terminal amino acid sequence with that of a 2-aminobenzoyl-CoA ligase of a denitrifying Pseudomonas sp. was found.

Acetate-CoA Ligase↗