DISULFIDE STRUCTURE OF A SUNFLOWER SEED ALBUMIN - CONSERVED AND VARIANT DISULFIDE BONDS IN THE CEREAL PROLAMIN SUPER-FAMILY

Disulphide mapping of a methionine-rich 2S albumin from sunflower seed s showed four intra-chain disulphide bonds which are homologous with t hose in a related heterodimeric albumin from lupin seeds (conglutin de lta). Similar conserved disulphide bonds are also present in alpha-gli adin and gamma-gliadin storage proteins of wheat, but a lower level of conservation is present in a further related group of proteins, the c ereal inhibitors of alpha-amylase and trypsin, These differences may r elate to the different functions of the proteins.