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Action of sodium aurothiomalate on erythrocyte membrane.
  1. J M Campbell,
  2. J Reglinski,
  3. W E Smith,
  4. D Porter,
  5. R D Sturrock
  1. Department of Pure and Applied Chemistry, Strathclyde University, Glasgow, United Kingdom.

    Abstract

    The number of sulphydryl groups on the erythrocyte membrane has been assessed as a function of nutritional status for two groups of patients, one receiving non-steroidal anti-inflammatory drugs (NSAIDs) and the other receiving sodium aurothiomalate (Myocrisin). The patients receiving NSAIDs had a significantly higher number of sulphydryl groups in both the glucose depleted and glucose activated states than the patients receiving sodium aurothiomalate. The study focuses on the hexose transport protein where there is a specific binding site for gold using the two sulphydryl residues on helices 11 and 12 of the protein. The data suggest that the strong binding of gold to the erythrocyte membrane occurs via thiol pairs rather than by isolated sulphydryl groups and that there are possibly two further binding sites for gold on the membrane, the identities of which are still unclear.

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