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.

本文详细地叙述了提取，分离、提纯豌豆球蛋白及其亚基的方法：用硼酸钠缓冲液提取豌豆球蛋白，用85%饱和度硫酸铵沉淀除去其它蛋白质杂质，再用凝胶柱进一步提纯，提纯的豌豆球蛋白通过DE52-纤维素阴离子树脂柱（8M尿素作为变性分离试剂）和S200凝胶柱（70%甲酸作为变性分离试剂）则可分离出豌豆球蛋白的各个亚基，试验结果还表明：在pH8.5时，33，000的亚基携带少量负电荷；而12，000的亚基携带大量负电荷。