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Article
June 1984

Effects of Echothiophate on Enzymatic Hydrolysis of Dipivefrin

Author Affiliations

From the Biochemistry Section, Allergan Pharmaceuticals, Irvine, Calif (Dr Anderson and Mr Richman); the Department of Ophthalmology, University of California at Irvine College of Medicine (Dr Anderson); and the Departments of Ophthalmology and Pharmacology, Mount Sinai School of Medicine, New York, and the Bronx Veterans Administration Hospital (NY) (Dr Mindel).

Arch Ophthalmol. 1984;102(6):913-916. doi:10.1001/archopht.1984.01040030733032
Abstract

• Dipivefrin is an antiglaucoma prodrug that is hydrolyzed to the active drug, epinephrine, by esterases in the cornea. Since cholinergic antiglaucoma agents are frequently used in combination with adrenergic agents, it was of interest to determine the effects of a commonly used irreversible cholinesterase inhibitor, echothiophate (Phospholine) iodide, on the dipivefrin esterases. In vitro studies showed that echothiophate is a competitive, reversible inhibitor of the soluble corneal dipivefrin esterases. In vivo studies substantiated the reversible nature of echothiophate inhibition, since no inhibition of dipivefrin hydrolysis could be detected 1% hours after echothiophate treatment and as early as 15 minutes after dipivefrin application.

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