Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.1.7 (acetylcholinesterase)
 28,390 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The immunization of rabbits with a paraoxon-HSA-conjugate resulted in an antibody response with titres of 1:25000 to 1:100000 of antisera dilution and average affinity constants K0 of 10(6) M-1 and heterogeneity indices of 0.8 to 0.9 calculated by means of the Sips equation. The serum cholinesterases and the erythrocyte acetylcholinesterase in immunized rabbits were protected against a stronger inhibition by parenteral application of paraoxon. An increase of blood glucose after paraoxon application to immunized rabbits could not be observed but was detectable in unimmunized animals.
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PMID:[Changes in the cholinesterase activity and glucose concentration in the blood induced by paraoxon in rabbits immunized against paraoxon]. 648 95

N-trans-p-coumaroyltyramine (CT) isolated from Physalis minima is a phenolic substance exhibiting many pharmacological activities like potent inhibition of acetyl cholinesterase, cell proliferation, platelet aggregation, and also antioxidant activity. Here, we have studied the binding of CT with HSA at physiological pH 7.2 by using fluorescence, circular dichroism spectroscopy, mass spectrometry, and molecular docking methods. From the fluorescence emission studies, the number of binding sites and binding constant were calculated to be 2 and (4.5 +/- 0.01) x 10(5) M(-1), respectively. The free energy change was calculated as -7.6 kcal M(-1) at 25 degrees C, which indicates the hydrophobic interactions of CT with HSA and is in well agreement with the computational calculations and molecular docking studies. The changes in the secondary structure of HSA after its complexation with the ligand were studied with CD spectroscopy, which indicated that the protein became partially unfolded. Also, temperature did not affect the HSA-CT complexes. The binding of CT with HSA was detected as 2 molecules bound to HSA was determined using micro TOF-Q mass spectrometry. Further, molecular docking studies revealed that CT was binding at subdomain IIA with hydrophobic interactions and also by hydrogen-bond interactions between the hydroxyl (OH) group of carbon-16 and carbon-2 of CT and Arg222, Ala291, Val293, and Met298 of HSA, with hydrogen-bond distances of 2.488, 2.811, 2.678, and 2.586 A, respectively.
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PMID:Interaction studies of coumaroyltyramine with human serum albumin and its biological importance. 2013 5