O'Connor C M, McGeeney K F
Biochim Biophys Acta. 1981 Apr 14;658(2):387-96. doi: 10.1016/0005-2744(81)90309-0.
Four alpha-amylase (1,4-alpha-D-glucan glucanohydrolase, EC 3.2.1.1) inhibitors were isolated from an albumin fraction of wheat flour by ion-exchange and gel-filtration chromatography. The purified inhibitors were characterized according to their electrophoretic mobilities, molecular weights, carbohydrate, content, sulphydryl content, susceptibility to proteolytic digestion and specificities in inhibiting human salivary and pancreatic alpha-amylases. The properties of these inhibitors ae compared to similar proteins isolated by other workers.
通过离子交换和凝胶过滤色谱法从小麦粉的白蛋白组分中分离出四种α-淀粉酶(1,4-α-D-葡聚糖葡聚糖水解酶,EC 3.2.1.1)抑制剂。根据其电泳迁移率、分子量、碳水化合物含量、巯基含量、对蛋白水解消化的敏感性以及抑制人唾液和胰腺α-淀粉酶的特异性对纯化的抑制剂进行了表征。将这些抑制剂的特性与其他研究人员分离出的类似蛋白质进行了比较。