【作者】 张桦； 王希东； 侯新东； 吴阳升； 张强； 石庆华； 喻梅辉；

【Author】 ZHANG Hua, WANG Xi-Dong, Hou Xin-dong,Wu Yang-sheng,ZHANG Qiang,XU Jian, SHI Qing-Hua YU Mei-Hui (Department of Biochemistry, College of Agricultural, Xinjiang Agricultural University, Urumqi 830052, China)

【机构】 新疆农业大学农学院生化教研室；

【摘要】 新疆红豆草胰蛋白酶抑制剂(简称OSTI)是1998年新发现的一种对胰蛋白酶具有强烈抑制作用的蛋白质,采用FPLC.Superose12柱层析,得到了经PAGE电泳纯化的OSTI.用SDS-PAGE方法测得分子量为2.2万左右Da.以BAPNA为底物,在最适条件下,测定反应速度——酶量曲线,测定结果表明,OSTI对胰蛋白酶的抑制作用属不可逆抑制,抑制摩尔比为1:2.修饰结果可见OSTI有Arg和Lys为中心的两个活性中心.测定OSTI的一级结构由203个氨基酸残基组成,属于Kunitz这一家族的新成员.更多还原

【Abstract】 The Trypsin Inhibitor from Onobrychis Saliva in Xinjiang(OSTI) was found in 1998. It is a kind of protein that can inhibit trypsin intensively, separating by FPLC superose 12, and obtaining purified OSTI by PAGE. Mensuration of molecular weigh of OSTI is around 22,000Da by SDS-PAGE.Taking BAPNA as the substrate, mensurating inhibit type and mole inhibitory ratio under the optimum conditions, the results of research indicate that OSTI has effect of irreversible inhibition on trypsin, and the mole ratio is about 1:2. The residue modification tests show that the active centers of OSTI are Arginine and Lysine.The primary structure of OSTI is made of 203 amino acid residues, OSTI is a new member belonging to the Kunitz family.更多还原