Lack of inhibition of human plasma cholinesterase and red cell acetylcholinesterase by antimony compounds including stibine
| Autor: | David E. Jane, S Anjum Hussain, Peter V. Taberner |
|---|---|
| Rok vydání: | 1998 |
| Předmět: |
Antimony
Male 0301 basic medicine Erythrocytes Stibine Health Toxicology and Mutagenesis chemistry.chemical_element Toxicology Sudden death Mice 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Chlorides Animals Cholinesterases Humans Cholinesterase Antimony trichloride 030102 biochemistry & molecular biology biology Infant Equipment Infant Newborn General Medicine Acetylcholinesterase Enzyme assay Biochemistry chemistry Enzyme inhibitor 030220 oncology & carcinogenesis biology.protein Colorimetry Cholinesterase Inhibitors Sudden Infant Death |
| Zdroj: | Human & Experimental Toxicology. 17:140-143 |
| ISSN: | 1477-0903 0960-3271 |
| DOI: | 10.1177/096032719801700303 |
| Popis: | 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 1073 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. |
| Databáze: | OpenAIRE |
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