Structural and immunochemical homologies between foxtail millet glutelin 60 kDa and starch granule-bound starch synthase proteins from rice, barley, corn and wheat grains.

Foxtail millet glutelin 60 kDa (MG60) was purified by preparative SDS-PAGE, and the N-terminal amino acid sequence was determined within 20 residues. The result demonstrated that the primary structure at N-terminal of MG60 was almost identical to those of the granule-bound starch synthase (GBSS) proteins from rice, barley, corn, wheat and potato. The existence of common epitopes among MG60 and GBSS proteins from these starch-storing cereals were corroborated by immunoblot analysis using antisera raised against MG60. These facts strongly suggest a close relationship between MG60-like glutelins and GBSS proteins.