IMMUNOCHEMICAL AND BIOCHEMICAL-IDENTIFICATION OF THE RICE SEED PROTEIN ENCODED BY CDNA CLONE A3-12

Previously isolated cDNA clone A3-12 that was expressed in E. coli as the fusion protein with Trp E showed immunoreactivity with the mouse a ntibody raised against isolated alpha-globulin from rice a seed. The N -terminal amino acid sequences determined for the purified alpha-globu lin and its tryptic peptides were identical with the deduced amino aci d sequence reported, except for two residues at the protein N terminus . An error in the reported sequence was confirmed by re-sequencing the cDNA, the nucleotide sequence for the two N-terminal residues being s hown to be CAGCTG and not CACGTG, Thus, the protein encoded by cDNA cl one A3-12 was identified to be the major rice seed globulin, alpha-glo bulin, with an apparent molecular mass of 26 kDa.