Inhibitors of animal cell-free protein synthesis from grains.
We described earlier the purification and properties of a protein (tritin) from wheat that enzymatically inhibits translation in cell-free systems from animals but not plants. In this report, we have examined 11 additional grains (Family Gramineae) and three other seeds for the presence of tritin-like proteins. In addition to wheat species, barley, oats, rye, triticale and corn were found to be sources of inhibitor; no inhibitor could be detected in rice, millet, sesame, alfalfa, mung bean or common bean seeds. The inhibitors from barley and rye were purified and found to differ from tritin with respect to heat inactivation, although they are similar to tritin with respect to molecular weight, behavior during purification and specific activity. The inhibitor from corn was purified and found to differ from tritin with respect to heat inactivation and molecular weight, although it is similar to tritin in behavior during purification and specific activity. These inhibitors constitute 2-17% of the total extractable protein in these grains. Thus, wheat, barley, rye and corn can serve as convenient sources of a family of closely related inhibitors of protein synthesis which, when conjugated with lectins, antibodies, or hormones, could prove useful as chimeric toxins.
D000818:Animals; D002286:Carcinoma, Ehrlich Tumor / Q000378:metabolism; D002523:Edible Grain; D007700:Kinetics; D051379:Mice; D010936:Plant Extracts / Q000494:pharmacology*; D010940:Plant Proteins / Q000302:isolation & purification / Q000494:pharmacology*; D014176:Protein Biosynthesis / Q000187:drug effects*; D013045:Species Specificity
D010936:Plant Extracts; D010940:Plant Proteins