The glutelin fraction was extracted from grain meals of rice (Guang-Ji 9) with 50 mM Tris-HCI buffer (pH 8.8) containing 6.0 M urea and 10 mM 2-mercaptoethanol. Poly-peptides of glutelin were separated and puri-fied by DEAE-cellulose and CM-cellulose under denaturing conditions. Analysis by two-dimensional gel electrophoresis showed that two major polypaptidcs of the rice glutclin fraction, M.W. 36000 and 22000, were linked in disulphide bonded pairs containing one M. W. 36000 and one M. W. 22000 subunit. Five acidic subunits (M. W. 36000) and six basic subunits (M. W. 22000) linked by disulphide bonds in the rice glutelin were also found. A partial amino acid sequence of the pu-rified M. W. 22000 glutelin subunit showed it to be homologous to the β-subunit of lcgu-rain, a storage protein which also contains disulphide-linked subunit pairs (M. W. 38000 and M. W. 20280). It is therefore proposed that the major component of rice glutelin is a legumin-like protein.