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. 1974 May;118(2):616–620. doi: 10.1128/jb.118.2.616-620.1974

Proteinase Produced by Chlamydia psittaci in L Cells

Gerald V Stokes a,1
PMCID: PMC246795  PMID: 4857192

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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