Sasaki T
Department of Food Science and Technology, School of Agriculture, Nagoya University, Aichi, Japan.
Biol Chem Hoppe Seyler. 1988 Nov;369(11):1235-41. doi: 10.1515/bchm3.1988.369.2.1235.
Amino-acid sequences of two basic chymotrypsin inhibitors from silkworm hemolymph (SCI-I and SCI-II) are determined. They are composed of each 62 amino-acid residues with differences in only two positions to each other. They both contain six half cystines in a similar arrangement as that of Kunitz-type proteinase inhibitor, except for the one amino-acid insertion in the first cysteine frame. The inhibitory activity of SCI-II against trypsin should be attributed to Lys44 displacing Gln44 in SCI-I which has no antitryptic activity.
测定了家蚕血淋巴中两种碱性胰凝乳蛋白酶抑制剂(SCI-I和SCI-II)的氨基酸序列。它们各自由62个氨基酸残基组成,彼此之间仅在两个位置上存在差异。它们都含有六个半胱氨酸,其排列方式与库尼茨型蛋白酶抑制剂相似,只是在第一个半胱氨酸框架中有一个氨基酸插入。SCI-II对胰蛋白酶的抑制活性应归因于Lys44取代了SCI-I中无抗胰蛋白酶活性的Gln44。