Reactivity of Some Nitrogen and Sulfur Mustards in Biologic Media.
Abstract
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)
Document Details
- Document Type
- Technical Report
- Publication Date
- Nov 01, 1971
- Accession Number
- AD0734828
Entities
People
- Benjamin Witten
- Charles E. Williamson