大鼠血清中的蛋白酶抑制剂。三种功能不同的胰蛋白酶抑制剂的纯化及部分特性分析。
Proteinase inhibitors in rat serum. Purification and partial characterization of three functionally distinct trypsin inhibitors.
作者信息
Kuehn L, Rutschmann M, Dahlmann B, Reinauer H
出版信息
Biochem J. 1984 Mar 15;218(3):953-9. doi: 10.1042/bj2180953.
Three different serine proteinase inhibitors were isolated from rat serum and purified to apparent homogeneity. One of the inhibitors appears to be homologous to alpha 1-proteinase inhibitor isolated from man and other species, but the other two, designated rat proteinase inhibitor I and rat proteinase inhibitor II, seem to have no human counterpart. alpha 1-Proteinase inhibitor (Mr 55000) inhibits trypsin, chymotrypsin and elastase, the three serine proteinases tested. Rat proteinase inhibitor I (Mr 66000) is active towards trypsin and chymotrypsin, but is inactive towards elastase. Rat proteinase inhibitor II (Mr 65000) is an effective inhibitor of trypsin only. Their contributions to the trypsin-inhibitory capacity of rat serum are about 68, 14 and 18% for alpha 1-proteinase inhibitor, rat proteinase inhibitor I and rat proteinase inhibitor II respectively.
从大鼠血清中分离出三种不同的丝氨酸蛋白酶抑制剂，并将其纯化至表观均一性。其中一种抑制剂似乎与人及其他物种中分离出的α1-蛋白酶抑制剂同源，但另外两种，即大鼠蛋白酶抑制剂I和大鼠蛋白酶抑制剂II，似乎没有对应的人类蛋白。α1-蛋白酶抑制剂（Mr 55000）可抑制所测试的三种丝氨酸蛋白酶：胰蛋白酶、胰凝乳蛋白酶和弹性蛋白酶。大鼠蛋白酶抑制剂I（Mr 66000）对胰蛋白酶和胰凝乳蛋白酶有活性，但对弹性蛋白酶无活性。大鼠蛋白酶抑制剂II（Mr 65000）仅是胰蛋白酶的有效抑制剂。它们对大鼠血清胰蛋白酶抑制能力的贡献分别约为：α1-蛋白酶抑制剂68%、大鼠蛋白酶抑制剂I 14%、大鼠蛋白酶抑制剂II 18%。
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