Boisen S
Z Lebensm Unters Forsch. 1983;176(6):434-9. doi: 10.1007/BF01042557.
The dominant trypsin inhibitors of the endosperm of barley, rye and wheat were investigated in a series of comparative studies. The barley and rye inhibitors showed a reaction of partial immunochemical identity, whereas no immunological cross-reactions between the wheat inhibitor and the inhibitors from barley and rye were detected. The molecular weight of the barley inhibitor is about 14,500, and of the rye and wheat inhibitors about 12,000. The three inhibitors had very similar amino acid compositions, but the wheat inhibitor seemed to contain nine disulfide bridges whereas the barley and rye inhibitor contain five and four, respectively. This may explain the higher stability of the wheat inhibitor towards proteolytic inactivation by pepsin and chymotrypsin. All three inhibitors were very stable to temperatures at 100 degrees C. The barley inhibitor was much less active against porcine trypsin, and especially human trypsin, than against bovine trypsin, whereas the inhibition by the rye and wheat inhibitor was less dependent on the origin of the enzyme.
在一系列比较研究中，对大麦、黑麦和小麦胚乳中的主要胰蛋白酶抑制剂进行了研究。大麦和黑麦抑制剂表现出部分免疫化学同一性反应，而未检测到小麦抑制剂与大麦和黑麦抑制剂之间的免疫交叉反应。大麦抑制剂的分子量约为14,500，黑麦和小麦抑制剂的分子量约为12,000。这三种抑制剂的氨基酸组成非常相似，但小麦抑制剂似乎含有九个二硫键，而大麦和黑麦抑制剂分别含有五个和四个二硫键。这可能解释了小麦抑制剂对胃蛋白酶和胰凝乳蛋白酶蛋白水解失活具有更高的稳定性。所有三种抑制剂在100摄氏度的温度下都非常稳定。大麦抑制剂对猪胰蛋白酶，尤其是人胰蛋白酶的活性比对牛胰蛋白酶的活性低得多，而黑麦和小麦抑制剂的抑制作用对酶的来源依赖性较小。
