Kreis M, Forde B G, Rahman S, Miflin B J, Shewry P R
J Mol Biol. 1985 Jun 5;183(3):499-502. doi: 10.1016/0022-2836(85)90017-8.
The major storage proteins (prolamins) of barley, rye and wheat are characterized by the presence of two or more unrelated structural domains, one of which contains repeated sequences. Because of this repetitive structure and their restricted distribution (only in grasses), it has been suggested that the prolamins are of recent origin. Contrary to this hypothesis, we show that parts of the non-repetitive domain of one group of prolamins are homologous with sequences present in a large group of seed proteins from monocotyledonous and dicotyledonous plants; including Bowman-Birk protease inhibitors, cereal inhibitors of alpha-amylase and trypsin, and 2 S globulin storage proteins of castor bean and oil seed rape. This implies an ancient origin for these non-repetitive domains. The origins of the repetitive domains are not known but may lie within the grasses.
大麦、黑麦和小麦的主要贮藏蛋白（醇溶蛋白）的特征是存在两个或更多不相关的结构域，其中一个含有重复序列。由于这种重复结构及其分布受限（仅存在于禾本科植物中），有人提出醇溶蛋白是近期起源的。与这一假设相反，我们发现一组醇溶蛋白的非重复结构域的部分与单子叶和双子叶植物的一大类种子蛋白中的序列同源；包括鲍曼-伯克蛋白酶抑制剂、谷物α-淀粉酶和胰蛋白酶抑制剂，以及蓖麻和油菜的2S球蛋白贮藏蛋白。这意味着这些非重复结构域起源古老。重复结构域的起源尚不清楚，但可能存在于禾本科植物中。
