Stokes G V
J Bacteriol. 1974 May;118(2):616-20. doi: 10.1128/jb.118.2.616-620.1974.
L cells (mouse fibroblasts) infected with Chlamydia psittaci (strain meningopneumonitis) produced a proteinase differing in solubility in ammonium sulfate from the proteinase of uninfected L cells. Synthesis of the enzyme was inhibited by chloramphenicol but not by cycloheximide, indicating that the new proteinase in infected L cells was synthesized by Chlamydia psittaci. The chlamydial proteinase had no demonstrable ion requirements and was not inhibited by a variety of inhibitors of proteinase activity. Gel filtration experiments suggested a molecular weight of approximately 250,000. The proteinase appeared in infected L cells at the time host cells began to die and the large chlamydial cells began to reorganize into small ones. Some possible functions for the chlamydial proteinase were proposed.
感染鹦鹉热衣原体（脑膜肺炎菌株）的L细胞（小鼠成纤维细胞）产生了一种蛋白酶，其在硫酸铵中的溶解度与未感染的L细胞的蛋白酶不同。氯霉素可抑制该酶的合成，但环己酰亚胺则不能，这表明感染的L细胞中的新蛋白酶是由鹦鹉热衣原体合成的。衣原体蛋白酶没有可证明的离子需求，并且不受多种蛋白酶活性抑制剂的抑制。凝胶过滤实验表明其分子量约为250,000。当宿主细胞开始死亡且大型衣原体细胞开始重组为小型细胞时，该蛋白酶出现在感染的L细胞中。文中还提出了衣原体蛋白酶的一些可能功能。
