Effects of Echothiophate on Enzymatic Hydrolysis of Dipivefrin

Janet A. Anderson, Joseph B. Richman, Joel S. Mindel

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

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.

Original languageEnglish
Pages (from-to)913-916
Number of pages4
JournalArchives of Ophthalmology
Volume102
Issue number6
DOIs
StatePublished - Jun 1984
Externally publishedYes

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