A case of hyper- and hypothyroidism induced by echothiophate iodide eye drops is presented. The thyroid dysfunction was due to excessive iodide intake from the eye drops.
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Molecules
March 2020
Kazan Federal University, Neuropharmacology Laboratory, Kremlevskaya str 18, 480002 Kazan, Russia.
Enzyme-catalyzed hydrolysis of echothiophate, a P-S bonded organophosphorus (OP) model, was spectrofluorimetrically monitored, using Calbiochem Probe IV as the thiol reagent. OP hydrolases were: the G117H mutant of human butyrylcholinesterase capable of hydrolyzing OPs, and a multiple mutant of phosphotriesterase, GG1, designed to hydrolyze a large spectrum of OPs at high rate, including V agents. Molecular modeling of interaction between Probe IV and OP hydrolases (G117H butyrylcholinesterase, GG1, wild types of and phosphotriesterases, and human paraoxonase-1) was performed.
View Article and Find Full Text PDFChem Res Toxicol
September 2019
Department of Physiological Sciences , Oklahoma State University, Stillwater , Oklahoma 74078 , United States.
The single residue mutation of butyrylcholinesterase (BChE) hydrolyzes a number of organophosphosphorus (OP) anticholinesterases. Whereas other BChE active site/proximal mutations have been investigated, none are sufficiently active to be prophylactically useful. In a fundamentally different computer simulations driven strategy, we identified a surface peptide loop (residues 278-285) exhibiting dynamic motions during catalysis and modified it via residue insertions.
View Article and Find Full Text PDFChem Biol Interact
June 2019
Kazan Federal University, Neuropharmacology Laboratory, Kremlevskaya Str, 18, Kazan, 420008, Russia. Electronic address:
A computer-designed mutant of human butyrylcholinesterase (BChE), N322E/E325G, with a novel catalytic triad was made. The catalytic triad of the wild-type enzyme (S198·H438·E325) was replaced by S198·H438·N322E in silico. Molecular dynamics for 1.
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