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.