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.
Takumi
K
K
Department of Food and Nutrition, Okayama Women's College, Kurashiki, Japan.
Udaka
J
J
Kimoto
M
M
Koga
T
T
Tsuji
H
H
D000595:Amino Acid Sequence; D002523:Edible Grain / Q000737:chemistry*; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D005983:Glutens / Q000737:chemistry*; D001467:Hordeum / Q000737:chemistry; D007120:Immunochemistry / Q000379:methods; D008970:Molecular Weight; D012275:Oryza / Q000737:chemistry; D008897:Panicum / Q000737:chemistry; D013214:Starch Synthase / Q000737:chemistry*; D014908:Triticum / Q000737:chemistry; D003313:Zea mays / Q000737:chemistry
D005983:Glutens; D013214:Starch Synthase