Biochemical Characterization of Rice Glutelin

Abstract

The 2 major subunits of rice glutelin, the acidic (.alpha.) and basic (.beta.) polypeptides were purified by chromatofocusing and cation exchange chromatography, respectively. The MW range of the .alpha. polypeptides was 28.5-30.8 kilodaltons and the MW range of the .beta. polypeptides was 20.6-21.6 kilodaltons. Electrofocusing in polyacrylamide gels showed that the isoelectric points of the .alpha. and .beta. polypeptides were 6.5 to 7.5 and 9.4 to 10.3, respectively. At least 12 polypeptides of the .alpha.-group and 9 polypeptides of the .beta.-group could be separated by electrofocusing. The amino acid compositions of whole glutelin and the purified .alpha. and .beta. subunits were analyzed. The .alpha. subunit contained more glutamic acid/glutamine, serine, and glycine, and less alanine, lysine, aspartic acid/asparagine, and isoleucine than the .beta. subunit. A comparison of the amino acid composition of rice glutelin subunits with those of the 11S proteins from 8 other plant species indicated that there is more similarity between the .beta. subunits than the .alpha. subunits of several diverse plant species.