Amouric M, Barthe C, Kopeyan C, Figarella C, Guy-Crotte O
Groupe de recherche sur les glandes exocrines, Marseille.
Biol Chem Hoppe Seyler. 1987 Nov;368(11):1525-32. doi: 10.1515/bchm3.1987.368.2.1525.
Protein X (PX) previously isolated from human pancreatic juice is an inactive protein of 14 kDa which has been shown to be a degradation product liberated by proteolysis of 19 kDa precursors. Polyclonal antibodies against P19 and PX were prepared in rabbits by injection of the two proteins purified by SDS polyacrylamide gel electrophoresis. These antibodies reacted with a form of trypsin 1 (DFP-trypsin 1) which was shown to be partly proteolysed. Immunological studies were performed with pancreatic juice proteins and partially purified trypsinogen 1 using antibodies directed against PX, P19 and trypsin 1. The results of immunoprecipitation and immunoadsorbent chromatography show that these different antisera recognized a protein of 25 kDa. Immunoblotting has permitted to characterize this protein as a trypsinogen 1-like molecule which would be a form of inert protein generated by uncontrolled trypsinogen activation.
先前从人胰液中分离出的蛋白质X（PX）是一种14 kDa的无活性蛋白质，已证明它是由19 kDa前体蛋白经蛋白水解释放出的降解产物。通过注射经SDS聚丙烯酰胺凝胶电泳纯化的这两种蛋白质，在兔体内制备了针对P19和PX的多克隆抗体。这些抗体与一种胰蛋白酶1（DFP - 胰蛋白酶1）的形式发生反应，该形式已显示出部分被蛋白水解。使用针对PX、P19和胰蛋白酶1的抗体，对胰液蛋白和部分纯化的胰蛋白酶原1进行了免疫学研究。免疫沉淀和免疫吸附色谱的结果表明，这些不同的抗血清识别出一种25 kDa的蛋白质。免疫印迹已将该蛋白质鉴定为一种类似胰蛋白酶原1的分子，它可能是由不受控制的胰蛋白酶原激活产生的一种无活性蛋白质形式。
