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Etomidate and plasma esterase activity in man and experimental animals
Pharmacology
|January 1, 1979
Summary
Etomidate hydrolysis in plasma varies significantly across species. Wistar rats exhibit marked hydrolysis due to an alliesterase, unlike most other tested mammals.
Area of Science:
- Pharmacology
- Biochemistry
- Veterinary Medicine
Background:
- Etomidate is an anesthetic agent.
- Understanding etomidate metabolism is crucial for its safe and effective use.
- Plasma hydrolysis is a potential metabolic pathway for etomidate.
Purpose of the Study:
- To investigate the in vitro hydrolysis of etomidate in plasma from various animal species.
- To identify the enzyme responsible for etomidate hydrolysis in susceptible species.
Main Methods:
- In vitro incubation of etomidate with plasma samples from humans, horses, cows, sheep, guinea pigs, white rabbits, brown rabbits, and Wistar rats.
- Analysis of hydrolysis products to determine the extent of etomidate metabolism.
- Investigating the role of specific enzymes, such as alliesterase and pseudocholinesterase.
Main Results:
- No significant etomidate hydrolysis was observed in human, horse, cow, sheep, guinea pig, or white rabbit plasma.
- Moderate hydrolysis occurred in brown rabbit plasma.
- Marked hydrolysis was detected in Wistar rat plasma, attributed to a single enzyme, alliesterase.
- Etomidate did not inhibit procaine hydrolysis by human plasma pseudocholinesterase.
Conclusions:
- Plasma etomidate hydrolysis is species-dependent, with Wistar rats showing significant metabolism.
- Aliesterase is identified as the primary enzyme responsible for etomidate hydrolysis in Wistar rat plasma.
- Etomidate does not interfere with the activity of human plasma pseudocholinesterase, suggesting minimal drug-drug interaction potential at this level.