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Related Concept Videos

Anticholinesterase Agents: Poisoning and Treatment01:26

Anticholinesterase Agents: Poisoning and Treatment

Anticholinesterases, also known as cholinesterase inhibitors, work by blocking the breakdown of acetylcholine, leading to its accumulation in the synaptic cleft. This accumulation indirectly enhances both muscarinic and nicotinic actions. These agents are classified as reversible or irreversible based on their mechanism of action.     
Irreversible agents form a strong bond with the cholinesterase enzyme, making it inactive. The breakdown of the phosphorylated enzyme is slower than the...
Indirect-Acting Cholinergic Agonists: Chemistry and Structure-Activity Relationship01:29

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Indirect-acting cholinergic agonists are agents that interact with the acetylcholinesterase enzyme in the synaptic cleft, preventing the breakdown of acetylcholine into choline and acetate. Consequently, the concentration of acetylcholine in the synaptic cleft increases. These agonists can be classified into reversible and irreversible inhibitors based on their duration of action.
Reversible inhibitors display short to medium durations of action. Short-acting agents include simple alcohols with...
Indirect-Acting Cholinergic Agonists: Mechanism of Action01:18

Indirect-Acting Cholinergic Agonists: Mechanism of Action

Indirect-acting cholinergic agonists work by interacting with an enzyme called acetylcholinesterase (AChE) in the synaptic cleft. They can be reversible or irreversible inhibitors and have different effects on the enzyme.
Reversible inhibitors like edrophonium bind to a specific part of the enzyme called the anionic catalytic site. They form noncovalent bonds, which means they are not strongly attached to the enzyme. This creates a temporary and less stable enzyme–inhibitor complex, leading to...
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Indirect-acting cholinergic agonists, or anticholinesterases, enhance the body's cholinergic activity by inhibiting acetylcholine's breakdown. They are categorized as reversible or irreversible agents based on their mechanism of action. They are further classified into short-acting, intermediate-acting, and long-acting agents based on their duration of action.
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Polyethylene terephthalate (PET) is a synthetic polymer widely utilized in the packaging industry, particularly for bottles and containers. Due to its chemical stability and durability, PET accumulates in the environment, contributing significantly to plastic pollution. It comprises repeating units of terephthalic acid and ethylene glycol, resulting in a semi-crystalline structure that is resistant to natural degradation processes.A notable breakthrough in plastic biodegradation came with the...

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Related Experiment Video

Updated: Jul 3, 2026

Nucleoside Triphosphates - From Synthesis to Biochemical Characterization
15:22

Nucleoside Triphosphates - From Synthesis to Biochemical Characterization

Published on: April 3, 2014

Dramatically stabilized phosphotriesterase-polymers for nerve agent degradation.

K E LeJeune1, A J Mesiano, S B Bower

  • 1Department of Chemical Engineering-Center for Biotechnology and Bioengineering, University of Pittsburgh, Pittsburgh, Pennsylvania 15261, USA.

Biotechnology and Bioengineering
|April 20, 1997
PubMed
Summary
This summary is machine-generated.

Immobilized phosphotriesterase (EC 3.1.8.1) in polyurethane foam shows enhanced stability and retains high activity. This enzyme system can degrade large quantities of nerve agent, offering a promising solution for detoxification.

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Published on: April 16, 2018

Area of Science:

  • Biocatalysis
  • Enzyme immobilization
  • Polymer science

Background:

  • Phosphotriesterase (EC 3.1.8.1) is crucial for hydrolyzing organophosphates.
  • Enzyme immobilization enhances stability and reusability for industrial applications.
  • Developing robust enzyme systems for hazardous substance degradation is essential.

Purpose of the Study:

  • To immobilize phosphotriesterase within a polyurethane foam matrix.
  • To evaluate the stability, activity, and functional integrity of the immobilized enzyme.
  • To assess the potential of immobilized phosphotriesterase for nerve agent degradation.

Main Methods:

  • Enzyme immobilization via prepolymer synthesis within a polyurethane foam.
  • Assessment of enzyme specific activity post-immobilization.
  • Evaluation of storage and thermal stability, including net stabilization energy.
  • Testing protease resistance and functional effects of immobilization.
  • Investigating the stabilizing effect of dimethyl sulfoxide.

Main Results:

  • Immobilized phosphotriesterase retained over 50% of its specific activity.
  • Significant increases in storage and thermal stability were achieved (net stabilization energy = 12.5 kJ/mol).
  • The immobilized enzyme demonstrated protease resistance and no loss of function.
  • Dimethyl sulfoxide showed a stabilizing effect on the enzyme system.
  • A projection indicated 2.5 kg of immobilized enzyme could degrade 30,000 tons of nerve agent annually.

Conclusions:

  • Polyurethane foam immobilization is an effective strategy for enhancing phosphotriesterase stability and activity.
  • The immobilized enzyme system exhibits remarkable thermal and storage stability without premodification.
  • The enzyme's resistance to proteases and functional integrity are maintained.
  • Organic solvent interactions may further stabilize the enzyme.
  • Immobilized phosphotriesterase presents a potent solution for large-scale nerve agent detoxification.