Disulphide structure of a sunflower seed albumin: conserved and variant disulphide bonds in the cereal prolamin superfamily.
Disulphide mapping of a methionine-rich 2S albumin from sunflower seeds showed four intra-chain disulphide bonds which are homologous with those in a related heterodimeric albumin from lupin seeds (conglutin delta). Similar conserved disulphide bonds are also present in alpha-gliadin and gamma-gliadin storage proteins of wheat, but a lower level of conservation is present in a further related group of proteins, the cereal inhibitors of alpha-amylase and trypsin. These differences may relate to the different functions of the proteins.
Egorov
T A
TA
Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russian Federation.
Odintsova
T I
TI
Musolyamov
A Kh
AKh
Fido
R
R
Tatham
A S
AS
Shewry
P R
PR
D055516:2S Albumins, Plant; D000595:Amino Acid Sequence; D052179:Antigens, Plant; D004220:Disulfides / Q000737:chemistry*; D006368:Helianthus / Q000737:chemistry*; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry*; D055315:Prolamins; D012639:Seeds / Q000737:chemistry*
D055516:2S Albumins, Plant; D052179:Antigens, Plant; D004220:Disulfides; D010940:Plant Proteins; D055315:Prolamins; C067568:methionine-rich 2S protein, Helianthus