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Z Binenfeld

Publications and source records attributed to Z Binenfeld.

14 recordsLinked to original sources
PubMed1997

Antidotal efficacy of quinuclidinium oximes against soman poisoning.

The efficiency of newly synthesized oxime derivatives of quinuclidinium were tested in vitro on soman inhibited acetylcholinesterase (AChE) of human erythrocytes and in vivo using soman poisoned mice. For this purpose, the inhibitory power of oximes (IC50), acute toxicity (LD50) as well as reactivating and protective capacities with respect to soman-inhibited AChE were determined for each of the oximes. All oximes tested were ineffective in vitro but protected mice very efficiently (BM-1 protects against 4LD50 of soman). The results indicate that the in vivo effectiveness of quinuclidinium oximes against soman poisoning may not be related to reactivation or protection of AChE but rather to some other mechanism of the cholinergic system.

Acetylcholinesterase↗
PubMed1988

Use of palladium(II) chloride as colour-forming reagent in determination of pralidoxime chloride in water and tablets.

Pralidoxime chloride (PAM-2Cl) has been determined spectrophotometrically in Britton-Robinson buffer solution at pH = 6.45; the method is based on measurement of the absorbance of the Pd(II)-pralidoxime complex at 327 nm. Studies of the composition of the complex by Job's continuous variation method, the molar ratio method and Bent-French's method yielded a Pd(II):pralidoxime ratio of 1:1. The conditional stability constant (K') of the complex at the optimum pH of 6.45 and an ionic strength (mu) of 0.3 M was found to be 10(5.2). The molar absorptivity was 1.05 x 10(4) 1 mol(-1) cm(-1). Beer's law was obeyed at concentrations up to 60 microM. The detection limit was 0.55 microg ml(-1). The relative standard deviation (N = 10) was 0.28-1.03%. The method was accurate and sensitive for the analysis of PAM-2Cl in water and tablets.

Journal Article↗
PubMed1987

Spectrophotometric determination of obidoxime chloride as its Pd(II) complex in water and injections.

It has been established that obidoxime chloride reacts with palladium(II) chloride in the pH range 3.9-8.0 and forms a yellow water-soluble (1:1) complex with maximum absorbance at 355 nm. By applying the methods of Sommer, Nash and Job involving non-equimolar solutions the conditional stability constant of the complex, at the optimum pH of 6.3 and an ionic strength mu = 0.55 M, is found to be 10(5.3). The molar absorptivity at 355 nm is 3.16 x 10(4) l mol(-1) cm(-1) at pH 6.3. Beer's law is obeyed up to 20 mumol l(-1) obidoxime chloride concentration. The detection limit of the method is 0.36 mug ml(-1). The relative standard deviation (n = 10) varies over the range 1.10-2.66%. The proposed method was found to be suitable for the accurate and sensitive analysis of obidoxime chloride in water and injection solutions.

Journal Article↗
PubMed1984

Reactivators of organophosphate-inhibited cholinesterase. 4-cycloalkylcarbonyl substituted bis-pyridinium monooximes.

Two isomeric cyclopentylcarbonyl and two cycloheptylcarbonyl derivatives of 2-hydroxyiminomethyl-1-[3-(1-pyridinio-2-oxapropyl]pyr idinium diiodide and 4-hydroxyiminomethyl-1-[3-(1-pyridinio-2-oxapropyl]pyr idinium diiodide were prepared and characterized by spectroscopic methods. The inhibitory power (I50) of the investigated oximes was determined using purified bovine erythrocyte AChE and human erythrocyte AChE. Percentage of reactivation after 30 min was estimated after inhibition of human erythrocyte AChE by sarin, VX, tabun, soman, and paraoxon. The in intro protective indices (p.i. and P50) against inhibition by soman have been calculated using bovine erythrocyte AChE for p.i. and human erythrocyte AChE for P50. Their I50 for human erythrocyte AChE varied from 1.4-9.8 (10(-4) mol . dm-3) and for bovine erythrocyte AChE in the range of 1.1-17 (10(-5) mol . dm-3). With 2 X 10(-5) mol . dm-3 oximes the percent of reactivation was: 0-17% for paraoxon-inhibited AChE, 9-49% for sarin-inhibited AChE, 16-65% for VX-inhibited AChE, 0-8% for tabun-inhibited AChE, and 0-4% for soman-inhibited AChE. The 2-hydroxyimino derivatives protect human erythrocyte AChE and purified bovine erythrocyte AChE from inhibition by soman.

Acetylcholinesterase↗
PubMed1982

Reactivators of organophosphate-inhibited cholinesterase. Phenylhydroxymethyl and cyclohexylhydroxymethyl substituted bis-pyridinium monooximes.

Eleven isomeric phenylhydroxymethyl and cyclohexylhydroxymethyl derivatives of 1-(2-hydroxyiminomethyl-1-pyridinio)-3-(1-pyridinio)-2-oxapropane diiodide and 1-(4-hydroxyiminomethyl-1-pyridinio)-3-(1-pyridinio)-2-oxapropane diiodide were prepared and characterized by spectroscopic methods and pKa values. The inhibitory power (I50) of the investigated oximes was determined on purified bovine erythrocyte AChE and human erythrocyte AChE. Percentage of reactivation after 30 min was estimated after inhibition of human erythrocyte AChE by sarin, VX, and paraoxon. The in vitro protective index against inhibition by soman has been calculated using bovine erythrocyte AChE. Their I50 for human erythrocyte AChE varied in the range of 9-61(10(-4) mol. dm-3) and for purified bovine erythrocyte AChE in the range of 11-57 (10(-5) mol . dm-3). With 2 X 10(-5) mol . dm-3 of oximes the percent of reactivation was: 0-63% for paraoxon inhibited AChE, 12-73% for sarin inhibited AChE and 11-80% for VX inhibited AChE. With the exception of 1-(2-hydroxyiminomethyl-1-pyridinio)-3-(4-phenylhydroxymethyl-1-pyridinio) -2-oxapropane diiodide (6) the derivatives of 4-hydroxyiminomethylpyridine are by far better reactivators. None of the compounds could protect purified bovine erythrocyte AChE from inhibition by soman.

Acetylcholinesterase↗
PubMed1979

1,3-Bispyridinium-dimethylether mono- and dioximes: synthesis, reactivating potency and therapeutic effect in experimental poisoning by organophosphorus compounds.

Nine bispyridinium oximes containing two pyridinium rings linked by dimethylether were synthesised. Each compound had on one of the pyridinium rings a hydroxyiminomethyl group in position 2 or 4, while the other ring was unsubstituted or had a methyl or a hydroxyiminomethyl group in position 2 or 4. The reactivating potency and therapeutic effect of the oximes were tested on two organophosphates: O,O-dimethyl-2,2-dichlorovinylphosphate (DDVP) and O-ethyl-S-(2-diisopropylaminoethyl)-methylphosphonothioate (VX). The reactivation was measured on human erythrocyte acetylcholinesterase and the therapeutic effect was evaluated on male albino rats. The oximes with a hydroxyiminomethyl group in position 4 in the pyridinium ring were good reactivators of both phosphorylated and phosphonylated acetylcholinesterase. They were also very effective given together with atropine against VX and DDVP poisoning. The compounds are almost as effective as PAM-2, but PAM-2 is less toxic.

Acetylcholinesterase↗
PubMed1966

[New nerve gases].

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Chemical Warfare↗