| Abstract: | Wool derivatives with sulfhydryl, thiosulfate, imidazole, pyrrolidone, or pyridine side chains were prepared and tested as potential scavengers for mercury salts in aqueous solution. More mercury is bound by these derivatives than by native wool or by certain commercial ion exchange resins under similar conditions. The presence of chloride ion, but not sulfate ion, in aqueous media decreased the extent of binding of mercuric chloride to both native and modified wools. The relative binding of mercuric chloride by various poly(amino acids) suggest that mercury is taken up by proteins by processes other than (or in addition to) specific combination with free functional groups. Two possibilities are suggested: the protein may act as a solid solvent for the mercurial, or the mercurial may form aggregated deposits within the protein after the specific binding sites have been occupied. These studies are intended to elucidate factors that govern mercury interaction with wool and other proteins and to develop improved scavengers for toxic metals. |
