Immunochemical examination of the surface physico-chemical properties of various dicotyledonous and monocotyledonous globulin seed storage proteins

Immunochemical analysis of the surface properties of seed globulins indicated that the 11S seed globulins of monocotyledonous and dicotyledonous plants possibly share some similarity in their primary structures, i.e. amino acid sequence on their surface topography as well in their structural conformation. Although homologies were found in all globulins, stronger antigenic responses were found to occur between the amaranth globulin antibody and the purified globulins from monocotyledonous than those originating from dicotyledonous seeds. Homologies in primary structure were found to occur almost exclusively in the ‘basic’ (20–27 000 Da) type subunit of the respective globulins. Data would imply that gene families encoding for these different proteins were derived from a common ancestral gene and must have been present before divergence of the angiosperms into dicotyledonous and monocotyledonous plants.