RYE INHIBITORS OF ANIMAL ALPHA-AMYLASES SHOW DIFFERENT SPECIFITIES, AGGREGATIVE PROPERTIES AND IGE-BINDING CAPACITIES THAN THEIR HOMOLOGS FROM WHEAT AND BARLEY

Three new members of the alpha-amylase/trypsin-inhibitor family of cer eal endosperm have been isolated from rye. N-terminal amino acid seque nce comparison revealed that two of the purified proteins were the rye homologues of the barley monomeric inhibitor (BMAI-1) previously desc ribed, while the other rye protein corresponded to one of the subunits of the barley and wheat heterotetrameric inhibitors. However, the inh ibitory specificities (active against human salivary alpha-amylase), a ggregative behaviours (mainly as dimeric forms) and IgE-binding capaci ties (not recognized by sera from allergic patients) of the rye inhibi tors were clearly different from those of their wheat and barley count erparts. These results indicate that homologous inhibitors may have di stinctive properties in different cereal species.