García-Casado G, Sánchez-Monge R, López-Otín C, Salcedo G
Unidad de Bioquímica, E. T. S. Ingenieros Agrónomos, Madrid, Spain.
Eur J Biochem. 1994 Sep 1;224(2):525-31. doi: 10.1111/j.1432-1033.1994.00525.x.
Three new members of the alpha-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 alpha-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.
已从黑麦中分离出谷物胚乳α-淀粉酶/胰蛋白酶抑制剂家族的三个新成员。N端氨基酸序列比较显示，其中两个纯化蛋白是先前描述的大麦单体抑制剂（BMAI-1）的黑麦同源物，而另一种黑麦蛋白则对应于大麦和小麦异源四聚体抑制剂的一个亚基。然而，黑麦抑制剂的抑制特异性（对人唾液α-淀粉酶有活性）、聚集行为（主要以二聚体形式）和IgE结合能力（未被过敏患者血清识别）与小麦和大麦对应物明显不同。这些结果表明，同源抑制剂在不同谷物物种中可能具有独特的特性。
