Abstract
THE activity of enzymes is modified—inhibited in most cases—by heavy-metal ions. Blockage of free sulphhydryl groups of the enzyme protein is held to be the cause of the inhibition1. A release of these groups, with subsequent recovery of enzyme activity, can be obtained in vitro by thiolic substances such as cystein or glutathione, which combine with the metallic ions. The sulphhydryl groups may be blocked also when the enzyme is in its original locus inside living cells. The inhibition of the enzyme is accompanied in this case by a breakdown of various cellular functions. This biochemical lesion (Peters), produced by a number of “substances thioloprives” (Bacq), can be prevented in many instances by mono- and di-thiols; but only in some cases, particularly in poisoning of the whole organism, can it be reversed.
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del CASTILLO-NICOLAU, J., HUFSCHMIDT, H. Reversible Poisoning of Nerve Fibres by Heavy-Metal Ions. Nature 167, 146–147 (1951). https://doi.org/10.1038/167146b0
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DOI: https://doi.org/10.1038/167146b0
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