Proteinase produced by Chlamydia psittaci in L cells.
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.
D000645:Ammonium Sulfate; D000818:Animals; D002689:Chlamydia / Q000201:enzymology*; D002701:Chloramphenicol / Q000494:pharmacology; D002850:Chromatography, Gel; D003513:Cycloheximide / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D006358:Hot Temperature; D007739:L Cells / Q000201:enzymology / Q000382:microbiology*; D051379:Mice; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000096:biosynthesis* / Q000378:metabolism; D012995:Solubility
D002701:Chloramphenicol; D003513:Cycloheximide; D010447:Peptide Hydrolases; D000645:Ammonium Sulfate