IN VITRO INTERACTION OF PROPANIDID AND SUXAMETHONIUM WITH POOLED HUMAN PLASMA CHOLINESTERASE

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 °C and pH 7.2 unit with butyrylthiocholine as substrate. Propanidid inhibited the enzyme in a non-competitive manner (/50 = 2.0 mmol...

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Bibliographic Details
Published in:British journal of anaesthesia : BJA 1979-03, Vol.51 (3), p.181-186
Main Authors: TAUSSIG, P.E., STOJAK, H.E., BENNETT, N.R.
Format: Article
Language:English
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Summary: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 °C and pH 7.2 unit with butyrylthiocholine as substrate. Propanidid inhibited the enzyme in a non-competitive manner (/50 = 2.0 mmol litre1; apparent Km 6.6 × 10–4 mollitre“1) as did suxamethonium (/60 = 4.4 mmol litre1; apparent Km 1.6 × 10–4 mol litre1). 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.
ISSN:0007-0912
1471-6771
DOI:10.1093/bja/51.3.181