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Enzyme Thermistor Devices
Published in Loïc J. Blum, Pierre R. Coulet, Biosensor Principles and Applications, 2019
In some cases the inhibition of the enzyme is irreversible. In this situation a reversible enzyme immobilization technique that allows simple replacement of spent enzyme is required. In one case this has been accomplished by reversibly binding cholinesterase (EC 3.1.1.7) to a concanavalin A-Sepharose column (3). A relatively sensitive determination of cholinesterase inhibitors has been made using butyrylcholine as substrate (17). The old enzyme is removed by injecting a pulse of 0.2 M glycine-HCl, pH 2.2. Fresh enzyme can then be immobilized on the column simply by injecting the enzyme preparation while the column remains in the enzyme thermistor apparatus.
Characterization of the antioxidant activity, total phenolic content, enzyme inhibition, and anticancer properties of Achillea millefolium L. (yarrow)
Published in Instrumentation Science & Technology, 2022
Nagihan Karaaslan Ayhan, Merve Goksin Karaaslan Tunc, Samir Abbas Ali Noma, Ali Kurucay, Burhan Ates
Acetylcholinesterase (AChE, E.C.3.1.1.7) is a key cholinesterase that plays an important role in cholinergic transmission. Enzymes are expressed in all tissue cells but have less activity. Acetylcholinesterase enzyme is primarily in muscles, brain, and cholinergic neurons and is responsible for the rapid hydrolysis of acetylcholine (ACh) at synapses.[24] Indeed, in the late phase of Alzheimer’s disease (AD), AChE levels increase significantly. Cholinesterase inhibitors or anti-cholinesterase prevent the breakdown of the neurotransmitter butyrylcholine or acetylcholine. The cholinergic system, which plays a significant role in the regulation of cognition, learning, and memory processes, has been extensively studied for the design of Alzheimer’s disease drugs.[25]
Docking assisted DNA-binding, biological screening, and nuclease activity of copper complexes derived from sulfonamides
Published in Journal of Coordination Chemistry, 2021
Arusa Akhtar, Muhammad Danish, Awais Asif, Muhammad Nadeem Arshad, Abdullah M. Asiri
Enzyme inhibitory potential of synthesized compounds was evaluated against two enzymes, i.e. AChE and BChE. Butyrylthiocholine iodide for BChE and acetylcholine iodide for AChE was used as substrate. The 100 μL enzyme (AChE and BChE) was added in 100 μL (5 mg/mL) of synthesized compound along with the addition of 0.5 mL sodium dihydrogen phosphate buffer (50 mM, pH = 8). The mixture was shaken well for 10 min and then added 50 μL DTNB and 50 μL of the substrate acetylcholine iodide and butyrylcholine iodide for AChE and BChE was added in the above solution mixture, respectively. Solutions were incubated at 37 °C for 30 min and then distilled water (1 mL) was added to each test tube. All the experiments were performed in triplicates and donepezil was used as standard drug to compare their results. After due time absorbance was recorded by a spectrophotometer at 410 nm [55]: where E stands for the activity of enzyme without sample and S stands for enzyme activity in the presence of the sample.
In vitro cholinesterase enzymes inhibitory potential and in silico molecular docking studies of biogenic metal oxides nanoparticles
Published in Inorganic and Nano-Metal Chemistry, 2018
Ali Talha Khalil, Muhammad Ayaz, Muhammad Ovais, Abdul Wadood, Muhammad Ali, Zabta Khan Shinwari, Malik Maaza
Elman’s procedure as previously described[27,28] was used to study the acetylcholinesterase (AChE; Sigma “101292679”) and butyrylcholinesterase (BChE; Sigma “101303874”) inhibition potential of the test samples in the concentration range of 1000 µg/mL to 62 µg/mL. Phosphate Buffer Saline was used for the dispersion of biogenic nanoparticles. The final concentrations of the enzymes were 0.03 U/mL and 0.01 U/mL for AChE and BChE, respectively. The substrate solutions DTNB (5,5-dithiobisnitrobenzoic acid; code “101261619”) (0.00022M), butyrylcholine iodide (BTchI; 0.0005M) and acetylcholine iodide (ATchI; 0.0005M) were all prepared in the distilled water and stored at 8 °C. For positive control Galanthamine hydrobromide (Sigma; GI660) prepared in methanol at the concentration of 10 µg/mL was used while in the case of negative control, the reaction mix was deprived of test sample.