Kopitar M, Brzin J, Drobnic-Kosŏrok M, Babnik J, Locnikar P, Turk V, Giraldi T, Sava G
Acta Biol Med Ger. 1982;41(1):75-82.
Leucocytes and spleen contain four different types of protein proteinase inhibitors. Two of them can be inactivated by cathepsin D. In this work biochemical and immunological studies of the inactivation of I-2 by cathepsin D are presented. Polyacrylamide gel electrophoretic examinations indicate that cathepsin D inactivates I-2 by hydrolysis of the inhibitor molecule. The conversion of the active inhibitor into inactive protein proceeds catalytically. The studies on the inhibitor mechanism of the isoinhibitors of I-1 type explain the unusual inhibitor property of this type of inhibitor to inhibit two different types of proteinases, cysteine and serine. The evidence suggests that the inhibitory mechanism is based on an active sulfhydryl group of the inhibitor which may interact with the disulfide bridge of the inhibited proteinase.
白细胞和脾脏含有四种不同类型的蛋白质蛋白酶抑制剂。其中两种可被组织蛋白酶D灭活。在这项工作中，展示了关于组织蛋白酶D使I-2失活的生化和免疫学研究。聚丙烯酰胺凝胶电泳检查表明，组织蛋白酶D通过水解抑制剂分子使I-2失活。活性抑制剂向无活性蛋白质的转化以催化方式进行。对I-1型同工抑制剂抑制机制的研究解释了这类抑制剂抑制两种不同类型蛋白酶（半胱氨酸蛋白酶和丝氨酸蛋白酶）的异常抑制特性。证据表明，抑制机制基于抑制剂的一个活性巯基，它可能与被抑制蛋白酶的二硫键相互作用。
