Reactivity of Some Nitrogen and Sulfur Mustards in Biologic Media.
Technical rept. Aug 65-May 71,
EDGEWOOD ARSENAL MD
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Certain nitrogen and sulfur mustards bind readily to blood constituents, thereby positioning them at macromolecular binding sites of low polarity. Because cyclization to form aziridinium and sulfonium ions is difficult in these environments, their rates of disappearance are decreased, the extent of which depends upon the degree of binding and the polarity of the binding sites. Serum albumin and hemoglobin contain hydrophobic binding sites and produce the largest rate inhibitions when these mustards are introduced into whole blood. Author
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