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06:13
Stepwise Dosing Protocol for Increased Throughput in Label-Free Impedance-Based GPCR Assays
Published on: February 21, 2020
Inhibitory activity of indolin-2-one derivatives on compound 48/80-induced histamine release from mast cells
G U Rüster1, B Hoffmann, M Hamburger
1Institute of Pharmacy, Friedrich-Schiller-University, Jena, Germany.
Die Pharmazie
|April 13, 2004
Abstract:
Four alkaloids, previously identified in Isatis species, were tested for their inhibitory effect on histamine release. Whereas tryptanthrin, indirubin and deoxyvasicinone did not inhibit histamine release, the effect of indolin-2-one exceeded that of the mast cell stabilizing drug disodium chromoglycate.
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01:29Indirect-Acting Cholinergic Agonists: Chemistry and Structure-Activity Relationship
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...
Reversible inhibitors display short to medium durations of action. Short-acting agents include simple alcohols with...
01:18Indirect-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...
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...