Drugs used to reverse the inactivation of cholinesterase caused by organophosphates or sulfonates. They are an important component of therapy in agricultural, industrial, and military poisonings by organophosphates and sulfonates.
Compounds which restore enzymatic activity by removing an inhibitory group bound to the reactive site of the enzyme.
Cholinesterase reactivator occurring in two interchangeable isomeric forms, syn and anti.
Compounds that contain the radical R2C=N.OH derived from condensation of ALDEHYDES or KETONES with HYDROXYLAMINE. Members of this group are CHOLINESTERASE REACTIVATORS.
Various salts of a quaternary ammonium oxime that reconstitute inactivated acetylcholinesterase, especially at the neuromuscular junction, and may cause neuromuscular blockade. They are used as antidotes to organophosphorus poisoning as chlorides, iodides, methanesulfonates (mesylates), or other salts.
An organophosphorus ester compound that produces potent and irreversible inhibition of cholinesterase. It is toxic to the nervous system and is a chemical warfare agent.
An enzyme that catalyzes the hydrolysis of ACETYLCHOLINE to CHOLINE and acetate. In the CNS, this enzyme plays a role in the function of peripheral neuromuscular junctions. EC 3.1.1.7.
Carbon-containing phosphoric acid derivatives. Included under this heading are compounds that have CARBON atoms bound to one or more OXYGEN atoms of the P(=O)(O)3 structure. Note that several specific classes of endogenous phosphorus-containing compounds such as NUCLEOTIDES; PHOSPHOLIPIDS; and PHOSPHOPROTEINS are listed elsewhere.
Pyridinium compounds are organic salts formed when pyridine, a basic heterocyclic organic compound, reacts with acids, resulting in a positively charged nitrogen atom surrounded by aromatic rings.
Drugs that inhibit cholinesterases. The neurotransmitter ACETYLCHOLINE is rapidly hydrolyzed, and thereby inactivated, by cholinesterases. When cholinesterases are inhibited, the action of endogenously released acetylcholine at cholinergic synapses is potentiated. Cholinesterase inhibitors are widely used clinically for their potentiation of cholinergic inputs to the gastrointestinal tract and urinary bladder, the eye, and skeletal muscles; they are also used for their effects on the heart and the central nervous system.
Agents counteracting or neutralizing the action of POISONS.
An organothiophosphate insecticide.
An organophosphate cholinesterase inhibitor that is used as a pesticide.
Chemicals that are used to cause the disturbance, disease, or death of humans during WARFARE.
Cholinesterase reactivator used as an antidote in alkyl phosphate poisoning.
Poisoning due to exposure to ORGANOPHOSPHORUS COMPOUNDS, such as ORGANOPHOSPHATES; ORGANOTHIOPHOSPHATES; and ORGANOTHIOPHOSPHONATES.
Organic compounds that contain phosphorus as an integral part of the molecule. Included under this heading is broad array of synthetic compounds that are used as PESTICIDES and DRUGS.

Re-activation of the peptidyltransferase centre of rabbit reticulocyte ribosomes after inactivation by exposure to low concentrations of magnesium ion. (1/149)

1. The larger subrivosomal particles of rabbit reticulocytes retained full activity in the puromycin reaction and in poly(U)-directed polyphenylalanine synthesis after 4h at 0 degrees C when buffered 0.5M-NH4Cl/10-30mM-MgCl2 was the solvent. 2. Activity in the puromycin reaction was diminished to approx 10% after 15-30 min at 0 degrees C when the concentration of MgCl2 was lowered to 2mM. 3. Activity was not restored when the concentration of MgCl2 was raised from 2mM to 10-30 mM at 0 degrees C. However, activity was recovered as measured by both assay systems when the ribosome fraction was heated to 37 degrees C at the higher concentrations of MgCl2. 4. Recovery of activity was noted during the course of the polyphenylalanine synthesis in 50 mM-KCl/5mM-MgCl2/25mM-Tris/HCl, pH 7.6, at 37 degrees C. Re-activation was slow at 20 degrees C and below. 5. No more than about 5% of the protein moiety of the subparticle was lost in 0.5M-NH4Cl on decreasing MgCl2 concentration from 10mM to 2mM. No proteins were detected in the supernatant fractions by gel electrophoresis after ribosomes were separated by differential centrifugation. The supernatant fraction was not essential for the recovery of activity. However, at higher (e.g. 1M) concentrations of NH4Cl, proteins were split from the subparticle. 6. The loss and regain of activity found on lowering and restoring the concentration of MgCl2 at 0.5M-NH4Cl appears to arise from a conformational change that does not seem to be associated with a loss and regain of particular proteins. 7. A 2% decrease in E260 was noticed when the concentration of Mg2+ was restored, and the change in the spectrum indicated a net increase of approx. 100A-U base-pairs per subribosomal particle. 8. When the concentration of Mg2+ was restored, S20,W of the subparticle remained at 52+/- 1S until the sample was incubated at 37 degrees C when S20,W increased to 56 +/- 1S compared with the value of 58 +/- 1S for the subparticle as originally isolated.  (+info)

A novel 35 kDa frog liver acid metallophosphatase. (2/149)

The lower molecular weight (35 kDa) acid phosphatase from the frog (Rana esculenta) liver is a glycometalloenzyme susceptible to activation by reducing agents and displaying tartrate and fluoride resistance. Metal chelators (EDTA, 1,10-phenanthroline) inactivate the enzyme reversibly in a time- and temperature-dependent manner. The apoenzyme is reactivated by divalent transition metal cations, i. e. cobalt, zinc, ferrous, manganese, cadmium and nickel to 130%, 75%, 63%, 62%, 55% and 34% of the original activity, respectively. Magnesium, calcium, cupric and ferric ions were shown to be ineffective in this process. Metal analysis by the emission spectrometry method (inductively coupled plasma-atomic emission spectrometry) revealed the presence of zinc, iron and magnesium. The time course of the apoenzyme reactivation, the stabilization effect and the relatively high resistance to oxidizing conditions indicate that the zinc ion is crucial for the enzyme activity. The presence of iron was additionally confirmed by the visible absorption spectrum of the enzyme with a shoulder at 417 nm and by the electron paramagnetic resonance line of high spin iron(III) with geff of 2.4. The active center containing only zinc or both zinc and iron ions is proposed. The frog liver lower molecular weight acid phosphatase is a novel metallophosphatase of lower vertebrate origin, distinct from the mammalian tartrate-resistant, purple acid phosphatases.  (+info)

Chemical modification of NADP-isocitrate dehydrogenase from Cephalosporium acremonium evidence of essential histidine and lysine groups at the active site. (3/149)

NADP-isocitrate dehydrogenase from Cephalosporium acremonium CW-19 has been inactivated by diethyl pyrocarbonate following a first-order process giving a second-order rate constant of 3.0 m-1. s-1 at pH 6.5 and 25 degrees C. The pH-inactivation rate data indicated the participation of a group with a pK value of 6.9. Quantifying the increase in absorbance at 240 nm showed that six histidine residues per subunit were modified during total inactivation, only one of which was essential for catalysis, and substrate protection analysis would seem to indicate its location at the substrate binding site. The enzyme was not inactivated by 5, 5'-dithiobis(2-nitrobenzoate), N-ethylmaleimide or iodoacetate, which would point to the absence of an essential reactive cysteine residue at the active site. Pyridoxal 5'-phosphate reversibly inactivated the enzyme at pH 7.7 and 5 degrees C, with enzyme activity declining to an equilibrium value within 15 min. The remaining activity depended on the modifier concentration up to about 2 mm. The kinetic analysis of inactivation and reactivation rate data is consistent with a reversible two-step inactivation mechanism with formation of a noncovalent enzyme-pyridoxal 5'-phosphate complex prior to Schiff base formation with a probable lysyl residue of the enzyme. The analysis of substrate protection shows the essential residue(s) to be at the active site of the enzyme and probably to be involved in catalysis.  (+info)

The p67(phox) activation domain regulates electron flow from NADPH to flavin in flavocytochrome b(558). (4/149)

An activation domain in p67(phox) (residues within 199-210) is essential for cytochrome b(558)-dependent activation of NADPH superoxide (O2(-.)) generation in a cell-free system (Han, C.-H., Freeman, J. L. R., Lee, T., Motalebi, S. A., and Lambeth, J. D. (1998) J. Biol. Chem. 273, 16663-16668). To determine the steady state reduction flavin in the presence of highly absorbing hemes, 8-nor-8-S-thioacetamido-FAD ("thioacetamido-FAD") was reconstituted into the flavocytochrome, and the fluorescence of its oxidized form was monitored. Thioacetamido-FAD-reconstituted cytochrome showed lower activity (7% versus 100%) and increased steady state flavin reduction (28 versus <5%) compared with the enzyme reconstituted with native FAD. Omission of p67(phox) decreased the percent steady state reduction of the flavin to 4%, but omission of p47(phox) had little effect. The activation domain on p67(phox) was critical for regulating flavin reduction, since mutations in this region that decreased O2(-.) generation also decreased the steady state reduction of flavin. Thus, the activation domain on p67(phox) regulates the reductive half-reaction for FAD. This reaction is comprised of the binding of NADPH followed by hydride transfer to the flavin. Kinetic deuterium isotope effects along with K(m) values permitted calculation of the K(d) for NADPH. (R)-NADPD but not (S)-NADPD showed kinetic deuterium isotope effects on V and V/K of about 1.9 and 1.5, respectively, demonstrating stereospecificity for the R hydride transfer. The calculated K(d) for NADPH was 40 microM in the presence of wild type p67(phox) and was approximately 55 microM using the weakly activating p67(phox)(V205A). Thus, the activation domain of p67(phox) regulates the reduction of FAD but has only a small effect on NADPH binding, consistent with a dominant effect on hydride/electron transfer from NADPH to FAD.  (+info)

Reversible alkaline inactivation of lignin peroxidase involves the release of both the distal and proximal site calcium ions and bishistidine co-ordination of the haem. (5/149)

Phanerochaete chrysosporium lignin peroxidase isoenzyme H2 (LiP H2) exhibits a transition to a stable, inactive form at pH 9.0 with concomitant spectroscopic changes. The Soret peak intensity decreases some 55% with a red shift from 408 to 412 nm; the bands at 502 nm and 638 nm disappear and the peak at 536 nm increases. The EPR spectrum changes from a signal typical of high spin ferric haem to an exclusively low spin spectrum with g=2.92, 2.27, 1.50. These data indicate that the active pentaco-ordinated haem is converted into a hexaco-ordinated species at alkaline pH. Room temperature near-IR MCD data coupled with the EPR spectrum allow us to assign the haem co-ordination of alkali-inactivated enzyme as bishistidine. Re-acidification of the alkali-inactivated enzyme to pH 6 induces further spectroscopic changes and generates an irreversibly inactivated species. By contrast, a pH shift from 9.0 to 6.0 with simultaneous addition of 50 mM CaCl(2) results in the recovery of the initial activity together with the spectroscopic characteristics of the native ferric enzyme. Incubating with 50 mM CaCl(2) at a pH between 6.0 and 9.0 can also re-activate the enzyme. Divalent metals other than Ca(2+) do not result in restoration of activity. Experiments with (45)Ca indicate that two tightly bound calcium ions per enzyme monomer are lost during inactivation and reincorporated during subsequent re-activation, consistent with the presence of two structural Ca(2+) ions in LiP H2. It is concluded that both the structural Ca(2+) ions play key roles in the reversible alkaline inactivation of LiP H2.  (+info)

In vitro and in vivo assessment of the effect of impurities and chirality on methamidophos-induced neuropathy target esterase aging. (6/149)

In vitro and in vivo studies evaluated neuropathy target esterase (NTE) inhibition and aging (i.e., loss of reactivation potential) by analytical and technical grade racemic and resolved L-(-) and D-(+) isomers of methamidophos (O,S-dimethyl phosphoramidothioate). For studies in vitro, microsomal protein from phenobarbital-induced livers was isolated from chick embryos and NTE inhibition assays were performed using chick embryo brain homogenate treated with 1 or 5 mM methamidophos (with and without metabolic enzymes); for studies in vivo, hens received 30 to 35 mg/kg methamidophos injected into the pectoral muscle. NTE aging in hens was assessed 24 h later or after 30 min to 1 h incubation in vitro using solutions of potassium fluoride (KF) reactivator. Technical methamidophos produced significantly higher levels of aged-inhibited NTE than analytical methamidophos or isolated optical isomers. In vivo, technical methamidophos produced 61% total NTE inhibition with 18% aged and 43% unaged NTE; hens receiving analytical grade averaged 6% aged, 52% unaged, and 58% total NTE inhibition. Results for 1 mM analytical methamidophos in vitro were 5% aged, 54% unaged, and 59% total inhibition; for 1 mM technical methamidophos, values averaged 11% aged, 50% unaged, and 60% total NTE inhibition. The degree of NTE aging obtained both in vivo and in vitro for the isolated D-(+) and L-(-) isomers never exceeded that obtained using analytical grade. These data indicate that impurities in methamidophos could contribute to OPIDN potential. The in vitro methodology described could be applied to first tier screening for detection of NTE inhibition and aging, thus reducing the need for whole-animal testing for OPIDN.  (+info)

Molecular chaperone properties of serum amyloid P component. (7/149)

The selective binding of serum amyloid P component (SAP) to proteins in the pathological amyloid cross-beta fold suggests a possible chaperone role. Here we show that human SAP enhances the refolding yield of denatured lactate dehydrogenase and protects against enzyme inactivation during agitation of dilute solutions. These effects are independent of calcium ions and are not inhibited by compounds that block the amyloid recognition site on the B face of SAP, implicating the A face and/or the edges of the SAP pentamer. We discuss the possibility that the chaperone property of SAP, or its failure, may contribute to the pathogenesis of amyloidosis.  (+info)

Studies of isopenicillin N synthase enzymatic properties using a continuous spectrophotometric assay. (8/149)

Isopenicillin N synthase (IPNS) from Aspergillus nidulans is a no-heme iron(II)-dependent oxygenase which catalyses, in a single reaction, the bicyclisation of delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-valine into isopenicillin N, the precursor of all other penicillins, cephalosporins and cephamycins. The IPNS reaction can be followed directly and continuously by a new assay which monitors the absorbance increase at 235 nm characteristic of penicillin nucleus formation. Using this assay, the effects of influential factors affecting the in vitro IPNS enzymatic reaction were investigated. Even under optimal conditions, enzyme inactivation occurred during catalysis. Iron(II) depletion and product inhibition were not the cause of this phenomenon, the addition of antioxidants or reducing agents failed to slow down inactivation or reactivate the enzyme. Therefore, this phenomenon appears to be irreversible and is attributed to oxidative damage caused to the enzyme by reactive oxygen species generated in solution during catalysis. Nevertheless, the steady-state kinetic parameters for the IPNS reaction were determined.  (+info)

Cholinesterase reactivators are a type of medication used to reverse the effects of certain types of poisoning, particularly organophosphate and carbamate pesticides, as well as nerve agents. These chemicals work by inhibiting the enzyme acetylcholinesterase, which normally breaks down the neurotransmitter acetylcholine in the body. This can lead to an overaccumulation of acetylcholine and result in symptoms such as muscle weakness, seizures, and respiratory failure.

Cholinesterase reactivators, also known as oximes, work by reactivating the inhibited enzyme and allowing it to resume its normal function. The most commonly used cholinesterase reactivator is pralidoxime (2-PAM), which is often administered in combination with atropine to treat organophosphate poisoning.

It's important to note that cholinesterase reactivators are not effective against all types of nerve agents or pesticides, and their use should be determined by a medical professional based on the specific type of poisoning involved. Additionally, these medications can have side effects and should only be administered under medical supervision.

Enzyme reactivators are substances or compounds that restore the activity of an enzyme that has been inhibited or inactivated. This can occur due to various reasons such as exposure to certain chemicals, oxidation, or heavy metal ions. Enzyme reactivators work by binding to the enzyme and reversing the effects of the inhibitor or promoting the repair of any damage caused.

One example of an enzyme reactivator is methionine sulfoxide reductase (Msr), which can reduce oxidized methionine residues in proteins, thereby restoring their function. Another example is 2-phenylethynesulfonamide (PESNA), which has been shown to reactivate the enzyme parkinsonism-associated deglycase (DJ-1) that is mutated in some cases of familial Parkinson's disease.

It is important to note that not all enzyme inhibitors can be reversed by reactivators, and the development of specific reactivators for particular enzymes is an active area of research with potential therapeutic applications.

Obidoxime chloride is a medication that belongs to the class of drugs known as oximes. It is used as an antidote for nerve agent and organophosphate poisoning. Obidoxime works by reactivating the inhibited acetylcholinesterase enzyme, which is essential for normal functioning of the nervous system. This enzyme can be inhibited by nerve agents and organophosphates, leading to an overstimulation of the nervous system that can result in symptoms such as muscle weakness, seizures, respiratory failure, and death.

Obidoxime is administered intravenously and works by breaking down the bond between the nerve agent or organophosphate and the acetylcholinesterase enzyme, allowing the enzyme to function normally again. It is important to note that obidoxime should be administered as soon as possible after exposure to a nerve agent or organophosphate in order to be effective.

It's important to mention that Obidoxime Chloride is not used frequently and only in specific situations, it requires medical supervision and administration by trained healthcare professionals.

Oximes are a class of chemical compounds that contain the functional group =N-O-, where two organic groups are attached to the nitrogen atom. In a clinical context, oximes are used as antidotes for nerve agent and pesticide poisoning. The most commonly used oxime in medicine is pralidoxime (2-PAM), which is used to reactivate acetylcholinesterase that has been inhibited by organophosphorus compounds, such as nerve agents and certain pesticides. These compounds work by forming a bond with the phosphoryl group of the inhibited enzyme, allowing for its reactivation and restoration of normal neuromuscular function.

Pralidoxime compounds are a type of antidote used to treat poisoning from organophosphate nerve agents and pesticides. These compounds work by reactivating the acetylcholinesterase enzyme, which is inhibited by organophosphates. This helps to restore the normal functioning of the nervous system and can save lives in cases of severe poisoning.

Pralidoxime is often used in combination with atropine, another antidote that blocks the effects of excess acetylcholine at muscarinic receptors. Together, these compounds can help to manage the symptoms of organophosphate poisoning and prevent long-term neurological damage.

It is important to note that pralidoxime must be administered as soon as possible after exposure to organophosphates, as its effectiveness decreases over time. This makes rapid diagnosis and treatment crucial in cases of suspected nerve agent or pesticide poisoning.

Sarin is a potent and deadly nerve agent, a type of organic compound called a phosphoro-organic fluid. It is a colorless, odorless, and tasteless liquid, which is also known as GB. Sarin is a human-made chemical warfare agent that is considered a weapon of mass destruction and is banned under the Chemical Weapons Convention of 1993.

Sarin works by inhibiting the enzyme acetylcholinesterase, which is responsible for breaking down the neurotransmitter acetylcholine in the body. This leads to an overaccumulation of acetylcholine at the neuromuscular junctions and synapses, causing uncontrolled muscle contractions, paralysis, respiratory failure, and ultimately death if not treated promptly.

Exposure to Sarin can occur through inhalation, skin contact, or ingestion. Symptoms of exposure include runny nose, tightness in the chest, difficulty breathing, nausea, vomiting, diarrhea, blurred vision, and confusion. Immediate medical attention is required for anyone exposed to Sarin, as antidotes such as atropine and pralidoxime can be administered to counteract its effects.

Acetylcholinesterase (AChE) is an enzyme that catalyzes the hydrolysis of acetylcholine (ACh), a neurotransmitter, into choline and acetic acid. This enzyme plays a crucial role in regulating the transmission of nerve impulses across the synapse, the junction between two neurons or between a neuron and a muscle fiber.

Acetylcholinesterase is located in the synaptic cleft, the narrow gap between the presynaptic and postsynaptic membranes. When ACh is released from the presynaptic membrane and binds to receptors on the postsynaptic membrane, it triggers a response in the target cell. Acetylcholinesterase rapidly breaks down ACh, terminating its action and allowing for rapid cycling of neurotransmission.

Inhibition of acetylcholinesterase leads to an accumulation of ACh in the synaptic cleft, prolonging its effects on the postsynaptic membrane. This can result in excessive stimulation of cholinergic receptors and overactivation of the cholinergic system, which may cause a range of symptoms, including muscle weakness, fasciculations, sweating, salivation, lacrimation, urination, defecation, bradycardia, and bronchoconstriction.

Acetylcholinesterase inhibitors are used in the treatment of various medical conditions, such as Alzheimer's disease, myasthenia gravis, and glaucoma. However, they can also be used as chemical weapons, such as nerve agents, due to their ability to disrupt the nervous system and cause severe toxicity.

Organophosphates are a group of chemicals that include insecticides, herbicides, and nerve gases. They work by inhibiting an enzyme called acetylcholinesterase, which normally breaks down the neurotransmitter acetylcholine in the synapse between nerves. This leads to an overaccumulation of acetylcholine, causing overstimulation of the nervous system and resulting in a wide range of symptoms such as muscle twitching, nausea, vomiting, diarrhea, sweating, confusion, and potentially death due to respiratory failure. Organophosphates are highly toxic and their use is regulated due to the risks they pose to human health and the environment.

Pyridinium compounds are organic salts that contain a positively charged pyridinium ion. Pyridinium is a type of cation that forms when pyridine, a basic heterocyclic organic compound, undergoes protonation. The nitrogen atom in the pyridine ring accepts a proton (H+) and becomes positively charged, forming the pyridinium ion.

Pyridinium compounds have the general structure of C5H5NH+X-, where X- is an anion or negatively charged ion. These compounds are often used in research and industry, including as catalysts, intermediates in chemical synthesis, and in pharmaceuticals. Some pyridinium compounds have been studied for their potential therapeutic uses, such as in the treatment of bacterial infections or cancer. However, it is important to note that some pyridinium compounds can also be toxic or reactive, so they must be handled with care.

Cholinesterase inhibitors are a class of drugs that work by blocking the action of cholinesterase, an enzyme that breaks down the neurotransmitter acetylcholine in the body. By inhibiting this enzyme, the levels of acetylcholine in the brain increase, which can help to improve symptoms of cognitive decline and memory loss associated with conditions such as Alzheimer's disease and other forms of dementia.

Cholinesterase inhibitors are also used to treat other medical conditions, including myasthenia gravis, a neuromuscular disorder that causes muscle weakness, and glaucoma, a condition that affects the optic nerve and can lead to vision loss. Some examples of cholinesterase inhibitors include donepezil (Aricept), galantamine (Razadyne), and rivastigmine (Exelon).

It's important to note that while cholinesterase inhibitors can help to improve symptoms in some people with dementia, they do not cure the underlying condition or stop its progression. Side effects of these drugs may include nausea, vomiting, diarrhea, and increased salivation. In rare cases, they may also cause seizures, fainting, or cardiac arrhythmias.

An antidote is a substance that can counteract the effects of a poison or toxin. It works by neutralizing, reducing, or eliminating the harmful effects of the toxic substance. Antidotes can be administered in various forms such as medications, vaccines, or treatments. They are often used in emergency situations to save lives and prevent serious complications from poisoning.

The effectiveness of an antidote depends on several factors, including the type and amount of toxin involved, the timing of administration, and the individual's response to treatment. In some cases, multiple antidotes may be required to treat a single poisoning incident. It is important to note that not all poisons have specific antidotes, and in such cases, supportive care and symptomatic treatment may be necessary.

Examples of common antidotes include:

* Naloxone for opioid overdose
* Activated charcoal for certain types of poisoning
* Digoxin-specific antibodies for digoxin toxicity
* Fomepizole for methanol or ethylene glycol poisoning
* Dimercaprol for heavy metal poisoning.

Disulfoton is a type of organophosphate pesticide that is used to control a variety of insects in agricultural settings. It functions as a cholinesterase inhibitor, disrupting the normal functioning of the nervous system in insects and leading to their death. However, disulfoton can also have toxic effects on humans and other mammals if ingested, inhaled, or absorbed through the skin. Therefore, it is important to use appropriate safety measures when handling this chemical.

The medical definition of Disulfoton is:

A colorless to light brown oily liquid organophosphate insecticide and acaricide. It is used for control of soil-inhabiting pests on a wide variety of crops, including corn, soybeans, potatoes, and ornamentals. Disulfoton is also used as a termiticide and a molluscicide. It acts by inhibition of cholinesterase. Exposure may occur through ingestion, inhalation, or skin absorption. Symptoms of exposure include nausea, vomiting, diarrhea, abdominal cramps, headache, dizziness, and tightness in the chest. Severe exposure can lead to respiratory failure, convulsions, unconsciousness, and death. Disulfoton is considered a highly toxic compound.

Paraoxon is the active metabolite of the organophosphate insecticide parathion. It functions as an acetylcholinesterase inhibitor, which means it prevents the breakdown of the neurotransmitter acetylcholine in the synaptic cleft. This leads to an accumulation of acetylcholine and overstimulation of cholinergic receptors, causing a variety of symptoms such as muscle weakness, increased salivation, sweating, lacrimation, nausea, vomiting, and potentially fatal respiratory failure.

Paraoxon is also used in research and diagnostic settings to measure acetylcholinesterase activity. It can be used to determine the degree of inhibition of this enzyme by various chemicals or toxins, including other organophosphate compounds.

Chemical warfare agents are defined as chemical substances that are intended or have the capability to cause death, injury, temporary incapacitation, or sensory irritation through their toxic properties when deployed in a military theater. These agents can be in gaseous, liquid, or solid form and are typically categorized based on their physiological effects. Common categories include nerve agents (e.g., sarin, VX), blister agents (e.g., mustard gas), choking agents (e.g., phosgene), blood agents (e.g., cyanide), and incapacitating agents (e.g., BZ). The use of chemical warfare agents is prohibited by international law under the Chemical Weapons Convention.

Trimedoxime is an antidote drug that is used to treat poisoning by organophosphate chemicals, which are commonly found in pesticides and nerve agents. It works by reactivating the acetylcholinesterase enzyme, which is inhibited by these toxic compounds, thereby restoring the normal functioning of the nervous system.

Medically, trimedoxime is classified as an oxime, a type of compound that can reverse the effects of organophosphate poisoning. It is often used in combination with atropine, another antidote drug that blocks the action of acetylcholine, a neurotransmitter that accumulates in the body due to organophosphate poisoning.

It's important to note that trimedoxime should only be administered under medical supervision and in accordance with established protocols for treating organophosphate poisoning. Improper use of this drug can lead to serious adverse effects.

Organophosphate (OP) poisoning refers to the toxic effects that occur after exposure to organophosphate compounds, which are commonly used as pesticides, nerve agents, and plasticizers. These substances work by irreversibly inhibiting acetylcholinesterase, an enzyme that breaks down the neurotransmitter acetylcholine in the nervous system. As a result, excessive accumulation of acetylcholine leads to overstimulation of cholinergic receptors, causing a wide range of symptoms.

The severity and type of symptoms depend on the dose, duration, and route of exposure (inhalation, ingestion, or skin absorption). The primary manifestations of organophosphate poisoning are:

1. Muscarinic effects: Excess acetylcholine at muscarinic receptors in the parasympathetic nervous system results in symptoms such as narrowed pupils (miosis), increased salivation, lacrimation, sweating, bronchorrhea (excessive respiratory secretions), diarrhea, bradycardia (decreased heart rate), and hypotension.
2. Nicotinic effects: Overstimulation of nicotinic receptors at the neuromuscular junction leads to muscle fasciculations, weakness, and paralysis. This can also cause tachycardia (increased heart rate) and hypertension.
3. Central nervous system effects: OP poisoning may result in headache, dizziness, confusion, seizures, coma, and respiratory depression.

Treatment for organophosphate poisoning includes decontamination, supportive care, and administration of antidotes such as atropine (to block muscarinic effects) and pralidoxime (to reactivate acetylcholinesterase). Delayed treatment can lead to long-term neurological damage or even death.

Organophosphorus compounds are a class of chemical substances that contain phosphorus bonded to organic compounds. They are used in various applications, including as plasticizers, flame retardants, pesticides (insecticides, herbicides, and nerve gases), and solvents. In medicine, they are also used in the treatment of certain conditions such as glaucoma. However, organophosphorus compounds can be toxic to humans and animals, particularly those that affect the nervous system by inhibiting acetylcholinesterase, an enzyme that breaks down the neurotransmitter acetylcholine. Exposure to these compounds can cause symptoms such as nausea, vomiting, muscle weakness, and in severe cases, respiratory failure and death.

Once the enzyme-OP complex has aged it is no longer regenerated by the common, oxime reactivators. The rate of this process is ... AChE is an enzyme involved with neurotransmission. Because of the severe decrease of the half-life of this enzyme, ... Nerve agents inhibit acetylcholine esterase (AChE) by forming an adduct with the enzyme via a serine residue on that enzyme. ... by the action of some oximes and thereby regenerate the enzyme. A second reaction type, one in which the enzyme-organophosphate ...
The therapy should be started early since otherwise there is maturation of the phosphorlyated enzyme. After 24hrs efficacy is ... Cholinesterase reactivators: oxime compounds are used, eg. Diacetyl monoxime, pralidoxime chloride, pralidoxime iodide, ... They are irreversible competitive inhibitors of enzyme Acetyl Cholinesterase. Site of action is myo-neural junction snd ...
... an enzyme essential to humans and other species. Design of effective AChE reactivators as antidotes to various ... First, reactivators are generally flexible in order to change from the ground state to the transition state for reactivation; ... Second, reactivation occurs upon binding of a reactivator to the phosphonylated AChE. Third, the phosphorous conjugate can ... These results offer insights into the reactivation mechanism of HI-6 and design of better reactivators. ...
... cosmetic surgery Kent cosmetic surgery London cosmetic surgery Sussex cosmetic surgery Tunbridge Wells enzyme reactivators HIFU ...
Enzyme Reactivators (Chemical Peels) New Generation Chemical Peels. Physiological. Refreshing.. 3D Cavitation Non-surgical ...
... enzyme inhibition for 2 minutes and subsequent treatment with the reactivator for 15 minutes).. CONCLUSION: Our work gives ... Cholinesterase Reactivators:chemistry, Enzymes, Immobilized:antagonists & inhibitors, Isomerism, Organophosphorus Compounds: ... The genes/enzymes (CYP2D6, COMT and PNMT) that are involved in the biosynthesis of morphine have variations that affect their ... OBJECTIVE: Clinical case of extremely elevated levels of alkaline phosphatase (ALP) enzyme detected in the 3rd trimester of ...
coord IM with specific enzyme (IM) but CHOLINESTERASE REACTIVATORS is available for reactivators of CHOLINESTERASES & ... Enzyme Reactivators - Preferred Concept UI. M0007522. Scope note. Compounds which restore enzymatic activity by removing an ... Compounds which restore enzymatic activity by removing an inhibitory group bound to the reactive site of the enzyme.. ...
Both in vitro and in silico studies conclude that K456 and K733 are unlikely to be used as reactivators of paraoxon-inhibited ... The reactivation of these inhibited enzymes is paramount for their normal function. Present study evaluates reactivation ... Organophosphates (OPs) irreversibly inhibit acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) enzymes. ... inhibited human-RBC-AChE and human-plasma-BChE in comparison to reported reactivator, pralidoxime (2-PAM). In vitro studies ...
Enzyme Reactivator 100% * Pralidoxime 79% * Antidote 66% * Area Under the Curve 66% ...
Enzyme Activators (0) * Enzyme Inhibitors (0) * Enzyme Reactivators (0) * Fibrin Modulating Agents (0) ...
The treatment comprises an antimuscarinic drug and an oxime reactivator of the inhibited enzyme. Oximes in use have quaternary ... Eight trans, anti- and trans, syn-isomers of oximes were tested as reactivators of nerve agent-inhibited AChE and BChE. Four ... New uncharged 2-thienostilbene oximes as reactivators of organophosphate-inhibited cholinesterases. Pharmaceuticals, 14 (11). ...
The organophosphorus inhibited activity is regained in the presence of cholinesterase reactivator. Moreover, the enzyme ... On the other hand, ATCh requires minimum 8-12 h staining time for detection of enzyme activity band following Karnovsky and ... Overnight incubation with the staining solution is required to understand the enzyme activity bands on gels. Therefore, the ... Our results prove that 1-NA is an alternative substrate of hemolysate cholinesterase which specifically detects the enzyme ...
The toxicity of OPNAs stems from covalent inhibition of the essential enzyme acetylcholinesterase (AChE), which reactivators ... Here, we present new strategies and tools for developing reactivators. We discover suitable inhibitor scaffolds by using an ... Our results show that new OPNA reactivators can be discovered rationally by exploiting detailed knowledge of the reactivation ... Reactivators are vital for the treatment of organophosphorus nerve agent (OPNA) intoxication but new alternatives are needed ...
All were effective reactivators of three OP-modified EEAChE conjugates showing 18-21% reactivation for DFP-inhibited AChE and ... Acute OP toxicity is primarily due to inhibition of acetylcholinesterase (AChE), an enzyme in the central and peripheral ... OP inhibition of AChE can be reversed using oxime reactivators but many show poor CNS penetration, indicating a need for new ... to 20-fold faster than the enzyme inhibited by S(P)R(C)- and S(P)S(C)-MSNP, and only 4% spontaneous reactivation was observed ...
OP inhibition of AChE can be reversed using oxime reactivators but many show poor CNS penetration, indicating a need for new ... Acute OP toxicity is primarily due to inhibition of acetylcholinesterase (AChE), an enzyme in the central and peripheral ... clinically viable reactivators. However, challenges exist on how to best measure restored AChE activity in vivo and assess the ...
Pralidoxime is a cholinesterase reactivator used to treat organophosphate poisoning. ... J Enzyme Inhib Med Chem. 2009 Jun;24(3):680-3. doi: 10.1080/14756360802328315. [Article] ... Jokanovic M, Prostran M: Pyridinium oximes as cholinesterase reactivators. Structure-activity relationship and efficacy in the ... If given within 24 hours,after organophosphate exposure, pralidoxime reactivates the enzyme cholinesterase by cleaving the ...
... it would bind to some of enzymes and decelerate the enzyme for designed time (e.g., use of this phenomena as a medical ... A study was done regarding the efficacy of oxime reactivators against AChE inhibited by guanitoxin. It was found that ... This occurs when the OPC phosphorylates the serine-203 residue of the enzyme. If the enzyme is not reactivated in time, a ... forming a salt bridge between the OP and the enzyme. This is called "Aging", and makes the inhibited enzyme resistant to ...
All about enzyme EC 3.1.1.7 - acetylcholine acetylhydrolase also known as acetylcholinesterase ... Enzymes. Enzyme classes:. EC 1: Oxidoreductases. EC 2: Transferases. EC 3: Hydrolases. EC 3.1. EC 3.1.1. EC 3.1.1.1. EC 3.1.1.2 ... 6u34: Binary Complex of Native Hache with Oxime Reactivator RS194B. *6u37: Structure of Vx-phosphonylated Hache in Complex with ... Enzyme kinetics. Inhibitors. Enzymes in industry. EC 3.1.1.7 - acetylcholine acetylhydrolase (acetylcholinesterase) 3D ...
Enzyme Activators. Enzyme Inhibitors. Enzyme Reactivators. Fibrin Modulating Agents. Heparin Antagonists. HIV Fusion Inhibitors ...
To exclude genetic or nutritional causes for the low enzyme activity, a cholinesterase reactivator, prallidoxime (4 pg per 500 ... The rate of recovery is determined by the degree of poisoning and by what caused it, and enzyme activity can remain depressed ... The enzyme activity in this sample did not differ from that of a freshly thawed standard. ... To ensure that high ambient temperatures had not reduced the cholinesterase activity, a standard solution of pure enzyme was ...
The enzyme activity was measured with acetylthiocholine as substrate. Enzyme-inhibitor dissociation constants for the catalytic ... were used as reactivators. When 1,1[oxybis-methylene)bis[4-(hydroxyimino)methyl] pyridinium dichloride (LuH6) and 1,1- ... These observations underline the importance of considering both genetic variability of enzyme isoform as well as enzyme level ( ... The data from mutant enzyme substantiate the involvement of edrophonium in protecting POX re-inhibition of reactivated enzyme ...
Enzyme Activators. *Enzyme Inhibitors. *Enzyme Reactivators. *Fibrin Modulating Agents. *Heparin Antagonists. *Membrane ... "Enzyme Activators" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical Subject ... This graph shows the total number of publications written about "Enzyme Activators" by people in this website by year, and ... Below are the most recent publications written about "Enzyme Activators" by people in Profiles. ...
Afterwards, an enzyme known as acetylcholinesterase (AChE) arrives to remove the ACh molecule. Without AChE, ACh molecules ... The biodistribution and pharmacokinetics of the oxime acetylcholinesterase reactivator RS194B in guinea pigs ... The scientists look for overall survivability and then, within an eight-hour window, they look at the enzymes present in the ... Nerve agents wreak havoc on the body by deactivating the AChE "cleanup" enzyme. The body is affected almost immediately, and an ...
Ref: J Enzyme Inhib Med Chem, 32:789, 2017 : PubMed. Abstract. ESTHER: Bosak_2017_J.Enzyme.Inhib.Med.Chem_32_789. PubMedSearch ... Title: Oximes: Reactivators of phosphorylated acetylcholinesterase and antidotes in therapy against tabun poisoning. Kovarik Z ... Ref: J Enzyme Inhib Med Chem, 23:521, 2008 : PubMed. Abstract. ESTHER: Bosak_2008_J.Enzyme.Inhib.Med.Chem_23_521. PubMedSearch ... All studied enzymes preferred inhibition by the R- over the S-bambuterol. The enlargement of the AChE choline binding site and ...
acetylcholinesterase ; coumarins ; enzyme reactivation ; Mitsunobu reaction ; organophosphorus compounds. Subjects:. NATURAL ... core through selected alkoxy side linkers attached at coumarin positions 6 or 7 to obtain a small set of possible reactivators ...
Reactivator. ?Reactivator. XREF. Inhibitor. Mutation. ?Mutation. XREF. Inhibitor. CID. ?CID. XREF. Inhibitor. ... Enzyme. ?Enzyme. XREF. Inhibitor. InChIKey. ?InChIKey. XREF. Inhibitor. CanonicalSMILES. ?CanonicalSMILES. XREF. Inhibitor. ...
Enzyme Activators. *Enzyme Inhibitors. *Enzyme Reactivators. *Fibrin Modulating Agents. *Heparin Antagonists. *Membrane ...
Inactivation of the enzyme allows acetylcholine to accumulate at the synapse, leading to overstimulation and disruption of ... The organophosphate-cholinesterase bond can spontaneously degrade, reactivating the enzyme, or can undergo a process called ... Organophosphates form an initially reversible bond with the enzyme cholinesterase. ...
This is possibly a result of a difference in enzyme sensitivity or a sex difference in the rate of metabolism. No other ... with reactivators of cholinesterase are effective antidotal agents for the acute toxic effects of fensulfothion. Short-term ... A summary of the significant features of the metabolic pathway of fensulfothion is shown in Figure 1. Effect on enzymes and ...
This period is crucial since treatment by reactivators such as ob. Posted on November 12, 2015. by admin ... We compared Unitrans distributions and gene ontology terms and identified enzyme differences among the treat ments especially ... This period is crucial since treatment by reactivators such as obidoxime and partially HI-6 are effective for paraoxon [18,19 ... alcohol oxidase enzyme (AOX) from Hansenula polymorpha, bovine serum albumin (BSA), Bradford reagent, all were from Sigma ...
  • Organophosphonates such as isopropyl metylphosphonofluoridate (sarin) are extremely toxic as they phosphonylate the catalytic serine residue of acetylcholinesterase (AChE), an enzyme essential to humans and other species. (proteopedia.org)
  • Structure of HI-6*sarin-acetylcholinesterase determined by X-ray crystallography and molecular dynamics simulation: reactivator mechanism and design. (proteopedia.org)
  • Organophosphates (OPs) irreversibly inhibit acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) enzymes. (simulations-plus.com)
  • Moreover, the enzyme activity bands formed using 1-NA proves the specificity of the substrate for hemolysate cholinesterase as in the presence of specific acetylcholinesterase inhibitors the band formation disappears. (who.int)
  • The toxicity of OPNAs stems from covalent inhibition of the essential enzyme acetylcholinesterase (AChE), which reactivators relieve via a chemical reaction with the inactivated enzyme. (ox.ac.uk)
  • Acute OP toxicity is primarily due to inhibition of acetylcholinesterase (AChE), an enzyme in the central and peripheral nervous system. (inrae.fr)
  • Organophosphorus compounds are known to inhibit the enzyme acetylcholinesterase (AChE). (stackexchange.com)
  • Acetylcholinesterase is important enzyme and its mechanism of function is well known. (stackexchange.com)
  • Organophosphates bind to the esteratic site of acetylcholinesterase, which results initially in reversible inactivation of the enzyme. (drugbank.com)
  • If given within 24 hours,after organophosphate exposure, pralidoxime reactivates the enzyme cholinesterase by cleaving the phosphate-ester bond formed between the organophosphate and acetylcholinesterase. (drugbank.com)
  • Afterwards, an enzyme known as acetylcholinesterase (AChE) arrives to remove the ACh molecule. (llnl.gov)
  • The most successful therapeutic strategy in the treatment of Alzheimer's disease (AD) is directed toward increasing levels of the neurotransmitter acetylcholine (ACh) by inhibition of acetylcholinesterase (AChE) and butyrylcholinesterase (BChE), the enzymes responsible for its hydrolysis. (inra.fr)
  • Nerve agents inhibit the enzyme acetylcholinesterase (AChE), which hydrolyzes the neurotransmitter acetylcholine (ACh) once ACh has finished activating receptors in neurons, muscles, and glands. (msdmanuals.com)
  • It is a nerve agent, interfering with normal functioning of the mammalian nervous system by inhibiting the enzyme cholinesterase. (wikipedia.org)
  • They are irreversible competitive inhibitors of enzyme Acetyl Cholinesterase. (pediatriconcall.com)
  • Cholinesterase reactivators: oxime compounds are used, eg. (pediatriconcall.com)
  • The organophosphorus inhibited activity is regained in the presence of cholinesterase reactivator. (who.int)
  • Our results prove that 1-NA is an alternative substrate of hemolysate cholinesterase which specifically detects the enzyme activity on gel rapidly. (who.int)
  • Pralidoxime is a cholinesterase reactivator used to treat organophosphate poisoning. (drugbank.com)
  • Cholinesterase activity was assessed in two blood samples by measuring the changes in absorbence at 405 nm (EPOS 5060 analyser) resulting when the chromogen 5,5'?dithiobis(4-nitrobenzoic acid) reacts with the thiocholine iodide produced by the action of the enzyme on a highly diluted sample of acetylthiocholine iodide. (dlawer.info)
  • To ensure that high ambient temperatures had not reduced the cholinesterase activity, a standard solution of pure enzyme was kept at 25oC for five days. (dlawer.info)
  • To exclude genetic or nutritional causes for the low enzyme activity, a cholinesterase reactivator, prallidoxime (4 pg per 500 ml blood), was introduced to reactivate the cholinesterase in the two samples and in the controls. (dlawer.info)
  • Prallidoxime will also remove organophosphates attached to the activity site of the cholinesterase causing an increase in enzyme activity. (dlawer.info)
  • Organophosphates form an initially reversible bond with the enzyme cholinesterase. (medscape.com)
  • The organophosphate-cholinesterase bond can spontaneously degrade, reactivating the enzyme, or can undergo a process called aging. (medscape.com)
  • Effect on enzymes and other biochemical parameters Fensulfothion, like other organophosphorothionate esters, is a weak cholinesterase inhibitor which, after being converted to the corresponding phosphate ester of fensulfothion is from 500 to 2 000 times more active in inhibiting cholinesterase. (inchem.org)
  • Pralidoxime chloride is a cholinesterase reactivator. (nih.gov)
  • OP pesticides inhibit carboxylic esterase enzymes including acetyl cholinesterase (AChE) and plasma cholinesterase (PChE) through binding to the esteratic site on the AChE molecule, phosphorylating the enzyme. (ac.ir)
  • Nerve agents inhibit acetylcholine esterase (AChE) by forming an adduct with the enzyme via a serine residue on that enzyme. (wikipedia.org)
  • Design of effective AChE reactivators as antidotes to various organophosphonates requires information on how the reactivators interact with the phosphonylated AChEs. (proteopedia.org)
  • this flexibility discourages determination of crystal structures of AChE in complex with effective reactivators that are intrinsically disordered. (proteopedia.org)
  • Second, reactivation occurs upon binding of a reactivator to the phosphonylated AChE. (proteopedia.org)
  • Present study evaluates reactivation potency of two newly developed oximes, K456 and K733, against paraoxon (POX)-inhibited human-RBC-AChE and human-plasma-BChE in comparison to reported reactivator, pralidoxime (2-PAM). (simulations-plus.com)
  • Both in vitro and in silico studies conclude that K456 and K733 are unlikely to be used as reactivators of paraoxon-inhibited AChE or BChE. (simulations-plus.com)
  • Eight trans, anti- and trans, syn-isomers of oximes were tested as reactivators of nerve agent-inhibited AChE and BChE. (irb.hr)
  • Our results show that new OPNA reactivators can be discovered rationally by exploiting detailed knowledge of the reactivation mechanism of OPNA-inhibited AChE. (ox.ac.uk)
  • OP inhibition of AChE can be reversed using oxime reactivators but many show poor CNS penetration, indicating a need for new clinically viable reactivators. (inrae.fr)
  • The hydrolysis reaction also protonates the nearby Histidine-447 at the active site of AChE, forming a salt bridge between the OP and the enzyme. (stackexchange.com)
  • Nerve agents wreak havoc on the body by deactivating the AChE "cleanup" enzyme. (llnl.gov)
  • Restoration of AChE levels occurs by spontaneous or induced reactivation of the enzyme and also by new enzyme synthesis (5). (ac.ir)
  • We discover suitable inhibitor scaffolds by using an activity-independent competition assay to study non-covalent interactions with OPNA-AChEs and transform these inhibitors into broad-spectrum reactivators. (ox.ac.uk)
  • Yet, there is a group inhibitors called irreversible inhibitors (and commonly known as suicide inhibitors because they kill the enzyme while get killing themselves), of which do not leave the active site once bound, unless an antidote is introduced. (stackexchange.com)
  • These results offer insights into the reactivation mechanism of HI-6 and design of better reactivators. (proteopedia.org)
  • The reactivation of these inhibited enzymes is paramount for their normal function. (simulations-plus.com)
  • A phenomenon of enzyme aging occurs which involves cleavage of a free radical from the inhibited enzyme, making it resistant to reactivation. (ac.ir)
  • Once the enzyme-OP complex has aged it is no longer regenerated by the common, oxime reactivators. (wikipedia.org)
  • These adducts may be decomposed hydrolytically or, for example, by the action of some oximes and thereby regenerate the enzyme. (wikipedia.org)
  • This is called "Aging", and makes the inhibited enzyme resistant to activation even by oximes. (stackexchange.com)
  • treatment with an oxime can regenerate the enzyme as long as the bond has not been further stabilized (a process termed aging) over time. (msdmanuals.com)
  • Inactivation of the enzyme allows acetylcholine to accumulate at the synapse, leading to overstimulation and disruption of nerve impulses. (medscape.com)
  • If the enzyme is not reactivated in time, a second reaction occurs, whereby one of the alkyl groups on the OP molecule is hydrolyzed off, giving the alcohol and the phosphorylated serine residue. (stackexchange.com)
  • This occurs when the OPC phosphorylates the serine-203 residue of the enzyme. (stackexchange.com)
  • The process of aging results in irreversible enzyme inactivation. (medscape.com)
  • Reactivators are vital for the treatment of organophosphorus nerve agent (OPNA) intoxication but new alternatives are needed due to their limited clinical applicability. (ox.ac.uk)
  • However, if you introduce a competitive inhibitor such as neostigmine (which is a reversible inhibitor), it would bind to some of enzymes and decelerate the enzyme for designed time ( e.g. , use of this phenomena as a medical treatment). (stackexchange.com)
  • As a result, choline group will be released and acetylated serine group would then release acetyl group as acetic acid in a moment by hydrolysis to reactivate the enzyme. (stackexchange.com)
  • Compounds which restore enzymatic activity by removing an inhibitory group bound to the reactive site of the enzyme. (bvsalud.org)
  • Compounds or factors that act on a specific enzyme to increase its activity. (uchicago.edu)
  • Enzyme Activators" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (uchicago.edu)
  • This review highlights some of the functional differences in the critical enzymes required for the biosynthesis of morphine that may affect human health. (nel.edu)
  • We compared Unitrans distributions and gene ontology terms and identified enzyme differences among the treat ments especially with regard to egg induced changes in transcript abundances. (inhibitorkit.com)
  • The presented assay showed complying results with reference method (standard spectrophotometry based on enzymes glucose oxidase and peroxidase inside plastic cuvettes) with linear dependence and correlation coefficient 0.999 in concentration range between 0 and 4 mmol/l. (nel.edu)
  • Binding to the esteratic site on the enzyme is stable and depending on the compound involved, it can last for hours or weeks (1). (ac.ir)
  • On the other hand, ATCh requires minimum 8-12 h staining time for detection of enzyme activity band following Karnovsky and Roots protocol. (who.int)
  • Once the inhibitor was released in an extended time period, enzyme will be reactivated. (stackexchange.com)
  • The treatment comprises an antimuscarinic drug and an oxime reactivator of the inhibited enzyme. (irb.hr)
  • Laboratory tests showed elevated (as much as a 10.5-fold increase) values of alkaline phosphatase enzyme, 94.05% of which was placental isoenzyme. (nel.edu)
  • Overnight incubation with the staining solution is required to understand the enzyme activity bands on gels. (who.int)
  • The enzyme activity in this sample did not differ from that of a freshly thawed standard. (dlawer.info)
  • Here, we present new strategies and tools for developing reactivators. (ox.ac.uk)
  • Clinical case of extremely elevated levels of alkaline phosphatase (ALP) enzyme detected in the 3rd trimester of gestation, the diagnostic and therapeutic procedures, delivery and puerperium are presented. (nel.edu)