ANTIGENIC HOMOLOGY BETWEEN AMARANTH GLUTELINS AND OTHER STORAGE PROTEINS

Amaranth seed proteins were sequentially extracted and partially chara cterized by electrophoresis and immunological analysis using three pol yclonal antibodies which were produced against an acidic subfraction o f amaranth globulin, an oat globulin, and an acidic subunit of rice gl utelin, Significant cross-reactivity was observed among glutelin and g lobulin fractions with these antibodies. Prolamin fraction did not rea ct. Data suggest that there is some structural homology between amaran th glutelin and globulin factions and that they could be legumin-like proteins because of their affinity with protein antibodies; such antib odies have been produced from legumin-like proteins. Two-dimensional e lectrophoretical analysis of a 32 kDa glutelin band clearly showed six acid components from pI 5.7 to 6.3; four of them cross-reacted with t he acidic subfraction of amaranth globulin antibody. These results con firm that there is homology between these acidic components (32 kDa) o f amaranth glutelin and the amaranth acidic subfraction of globulin.