In vitro interaction of propanidid and suxamethonium with pooled human plasma cholinesterase. A kinetic study.

Abstract:

:Human plasma cholinesterase (E.C. 3.1.1.8) was shown to be inhibited by physiological concentrations of propanidid and suxamethonium using a colourimetric assay at 25 degrees C and pH 7.2 unit with butyrylthiocholine as substrate. Propanidid inhibited the enzyme in a non-competitive manner (I50 = 2.0 mmol litre-1; apparent Km = 6.6 X 10(-4) mol litre-1) as did suxamethonium (I50 = 4.4 mmol litre-1; apparent Km = 1.6 X 10(-4) mol litre-1). Combined inhibition produced Km 3.0 X 10(-3) mol litre-1. The binding of these drugs to specific anionic sites in the vicinity of the active centre is thought to result in stereochemical changes in the enzyme. This mechanism and its relevance to the augmentation of the neuromuscular blockade produced by suxamethonium in the presence of propanidid is discussed.

journal_name

Br J Anaesth

authors

Taussig PE,Stojak HE,Bennett NR

doi

10.1093/bja/51.3.181

subject

Has Abstract

pub_date

1979-03-01 00:00:00

pages

181-6

issue

3

eissn

0007-0912

issn

1471-6771

pii

S0007-0912(17)44993-2

journal_volume

51

pub_type

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