ANALYSIS OF ADZUKI BEAN SEED PROTEIN BY PARTIAL AMINO-ACID SEQUENCING OF POLYPEPTIDE SEPARATED ON 2-DIMENSIONAL GEL

Adzuki bean (Vigna angularis (WILLD.) OHWI et OHASHI) seed proteins were analyzed by two-dimensional polyacrylamide gel electrophoresis and the N-terminal or internal amino acid sequence determined. Several analyzed proteins were identified and mapped on two-dimensional polyacrylamide gel, as proteins homologous to legumin, vicilin and glycinin by homology search. All varieties which were analyzed in this experiment showed heterogeneities only in adzuki-vicilins on the electrophoresis profiles. Additionally, proteins whose N-terminal amino acid sequences were homologous to the internal amino acid sequences of pea vicilin were identified on 2D-PAGE profiles, and a deficient variety of these proteins was also identified in 15 varieties of adzuki bean.