Nakagawa H, Hirata K
FEBS Lett. 1986 Oct 20;207(1):58-62. doi: 10.1016/0014-5793(86)80012-6.
Two species of cysteine-proteinase inhibitors (CPIs) have been purified to homogeneity from exudate in the carrageenin-induced inflammation in rats. The exudate CPIs were separated into two forms (named CPI-1 and -2) in affinity chromatography on S-carboxymethyl-papain-Sepharose, the final stage of purification. CPI-1 and -2 gave different mobilities in polyacrylamide gel electrophoresis (PAGE), probably because of different isoelectric points (pI 4.47 for CPI-1 and pI 4.21 for CPI-2). Both CPI-1 and -2 showed immunological identity in double immunodiffusion and same molecular mass of 68 kDa when analysed by SDS-PAGE. These results indicate that CPI-1 and -2 are very similar but distinct CPIs. CPI-1 and -2 are acute-phase reactants and probably represent two species of T-kininogens having inhibitory activity toward cysteine proteinases.
从角叉菜胶诱导的大鼠炎症渗出物中已将两种半胱氨酸蛋白酶抑制剂（CPI）纯化至同质。在纯化的最后阶段，即S-羧甲基木瓜蛋白酶-琼脂糖亲和层析中，渗出物CPI被分离为两种形式（命名为CPI-1和-2）。CPI-1和-2在聚丙烯酰胺凝胶电泳（PAGE）中具有不同的迁移率，这可能是由于等电点不同（CPI-1的pI为4.47，CPI-2的pI为4.21）。通过双免疫扩散分析，CPI-1和-2显示出免疫同一性，并且通过SDS-PAGE分析时具有相同的68 kDa分子量。这些结果表明，CPI-1和-2是非常相似但又不同的CPI。CPI-1和-2是急性期反应物，可能代表两种对半胱氨酸蛋白酶具有抑制活性的T-激肽原。
