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Lack of inhibition of human plasma cholinesterase and red cell acetylcholinesterase by antimony compounds including stibine

Department of Pharmacology, University of Bristol, School of Medical Sciences, University Walk, Bristol BS8 1TD, UK

David E Jane

Department of Pharmacology, University of Bristol, School of Medical Sciences, University Walk, Bristol BS8 1TD, UK

Peter V Taberner

Department of Pharmacology, University of Bristol, School of Medical Sciences, University Walk, Bristol BS8 1TD, UK

1 The toxic gas hypothesis proposes exposure to stibine (antimony trihydride) generated from microbial contamination of cot mattress materials as a possible cause of unexplained death in infancy (SIDS) as a consequence of cholinesterase inhibition. We have measured the direct effects of antimony compounds including stibine on the activity of plasma cholinesterase, red blood cell acetylcholinesterase (AChE) and mouse neuronal AChE in vitro.

2 Colorimetric assays for the different esterases with potassium antimonyl tartrate or antimony trichloride at concentrations up to 10^{7 3} M inthepresenceof substrate concentrations sufficient to produce 80% of the maximum reaction rate produced no inhibition of enzyme activity. Exposure of enzyme preparations to stibine gas at concentrations sufficient to cause denaturation of red cell haemogloblin caused no measurable inhibition of esterase activity.

3 We conclude that stibine gas or soluble antimony compounds are not capable of inhibiting cholinesterase activity at toxicologically relevant concentrations.

Key Words: SIDS • stibine • cholinesterase • toxic gas hypothesis

Human & Experimental Toxicology, Vol. 17, No. 3, 140-143 (1998)
DOI: 10.1177/096032719801700303


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