Tunek_1988_Biochem.Pharmacol_37_3867

Reference

Title : Hydrolysis of 3H-bambuterol, a carbamate prodrug of terbutaline, in blood from humans and laboratory animals in vitro - Tunek_1988_Biochem.Pharmacol_37_3867
Author(s) : Tunek A , Levin E , Svensson LA
Ref : Biochemical Pharmacology , 37 :3867 , 1988
Abstract :

Tritiated bambuterol, a bis-dimethylcarbamate prodrug of terbutaline, was incubated in vitro with blood from both sexes of the following species: man, guinea pig, rat, mouse, dog and rabbit. The rates of hydrolysis of bambuterol to its monocarbamate derivative and further to terbutaline were measured. Large species variations were observed, e.g. blood from two of the human subjects was 15-fold more active than blood from the male rats. The rate of terbutaline formation as a function of initial bambuterol concentration was investigated in human plasma, and was found to describe a bell-shaped curve. Several pieces of evidence indicated that butyrylcholinesterase (EC 3.1.1.8) is the blood enzyme predominantly responsible for hydrolysis of bambuterol, although minor contributions from other esterases cannot be excluded. An exception may be blood from the rabbit, where the kinetics of the hydrolysis was different than in blood from the other species. The kinetics of bambuterol hydrolysis is discussed on basis of the established mechanism of carbamate interactions with cholinesterases, and the high affinity of bambuterol for butyrylcholinesterase.

PubMedSearch : Tunek_1988_Biochem.Pharmacol_37_3867
PubMedID: 3190733

Related information

Inhibitor Bambuterol
Substrate Bambuterol    Bambuterol

Citations formats

Tunek A, Levin E, Svensson LA (1988)
Hydrolysis of 3H-bambuterol, a carbamate prodrug of terbutaline, in blood from humans and laboratory animals in vitro
Biochemical Pharmacology 37 :3867

Tunek A, Levin E, Svensson LA (1988)
Biochemical Pharmacology 37 :3867