The action of sodium salicylate and related compounds on the proteins of the groundnut (Arachis hypogaea)

Abstract

AbstractThe action of sodium salicylate on arachin and conarachin II has been investigated by viscosity and sedimentation velocity techniques. Considerable evidence for the occurrence of aggregation of the protein has been obtained. It appears that the salicylate ion first penetrates the protein molecule causing a modification of the internal linkages resulting in an opening up of the molecule. This would lead to the exposure of many more active groups which probably then react with active groups on other molecules. The effect of the salicylate ion was more pronounced at lower pH values (ca. 6‐7) and higher ionic strengths (ca. 1.0). Considerably greater effects were observed with conarachin II than with arachin, indicating that the arachin molecule is probably more strongl bound internally. The effect of a number of other sodium salts of organic acids on conarachin II was examined, and it appears that the action of any organic anion depends on the nonpolar portion of the molecule as well as on the polar groups.