POLYPEPTIDE COMPOSITION AND LOCALIZATION OF PROLAMIN AND GLUTELIN IN RICE COLEOPTILES

The method of unidimensional electrophoresis in SDS-PAAG has been used to study polypeptide composition and localization of the main storage proteins of the rice caryopsis (Oryza sativa L.)-prolamine and glutel in. Rice prolamine is a complex heterogeneous protein represented by t ypical and atypical sulfur-containing prolamines that differ in their relationship to extracting solutions (isopropyl alcohol and 2 M urea), in the action of reducing agents, and in their localization in storag e ultra-structures. Rice glutelin is a multicomponent protein represen ted by groups of acidic and basic polypeptides in the reduced and unre duced states. Separate components of both prolamine and glutelin are l ocalized in different storage ultrastructures. Protein bodies of the P B 1 type serve as the site of accumulation of typical prolamines and c ertain high-molecular-weight acidic polypeptides of glutelin.