
Rye Inhibitors of Animal α‐amylases Show Different Specifities, Aggregative Properties and IgE‐binding Capacities than Their Homologues from Wheat and Barley
Author(s) -
GarcíaCasado Gloria,
SánchezMonge Rosa,
LópezOtín Carlos,
Salcedo Gabriel
Publication year - 1994
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1994.00525.x
Subject(s) - amylase , biology , chemistry , food science , biochemistry , enzyme
Three new members of the α‐amylase/trypsin‐inhibitor family of cereal endosperm have been isolated from rye. N‐terminal amino acid sequence comparison revealed that two of the purified proteins were the rye homologues of the barley monomeric inhibitor (BMAI‐1) previously described, while the other rye protein corresponded to one of the subunits of the barley and wheat heterotetrameric inhibitors. However, the inhibitory specificities (active against human salivary α‐amylase), aggregative behaviours (mainly as dimeric forms) and IgE‐binding capacities (not recognized by sera from allergic patients) of the rye inhibitors were clearly different from those of their wheat and barley counterparts. These results indicate that homologous inhibitors may have distinctive properties in different cereal species.