1) Institute of Agronomy, National Taiway University, Roosevelt Road, Taipei

2) Institute of Botany, Academia Sinica, Nankang, Taipei, Taiwan, ROC

Glutelin is the major storage protein of rice and is processed post- translationally from 57 KD precursor into the α and β subunits with molecular weight 37-39 KD and 21-22 KD, respectively (Yamagata et al. 1982). By isoelectric focusing, it can also be dissolved into groups of acidic and basic bands that correspond to the α and β subunits, respectively. The acidic bands were separated into several bands (Wen and Luthe 1985). The two- dimensional separation of the α subunit of glutelin from 13 genomic species of Oryza is reported in this note. It revealed That in the species examined there were a number of different polypeptides that were heterogeneous in both molecular weight and isoelectric point (pI value), as shown in Fig. 1 and Table 1. Polypeptides with 30/7.5, 30/7.3 and 30/7.1, which were found in most species may be considered as the main constitutive. Thus, similarity and diversity in glutelin α subunit were disclosed among Oryza species.