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SummaryFoxtail millet glutelin 60kDa (MG6O) 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. Key Words foxtail millet, glutelin 60kDa, N-terminal amino acid sequence, starch gran ule-bound starch synthase, antigenic homology.Our previous paper (1) indicated that the prolamins from foxtail (Italian), proso (Common) and sawa (Japanese) millet cultivars contained common epitopes among them. Since then, however, little information on the physico-or immuno-chemical properties of the mil let storage proteins has been published so far as we know. Miflin and Shewry (2) have proposed that glutelin proteins serve a metabolic and/or structural role rather than a storage function in some cereals. Recently, we purified a polypeptide a component with a molecular mass (MM) of 60 kDa (referred to as MG60) from the urea-soluble glutelin of a foxtail millet cultivar. Then, the N-terminal amino acid sequence of MG60 was determined by the method of Matsudaira (3) in order to obtain the first clue about the function of the newly obtained glutelin component.

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