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. 1995 Jun;63(6):2387–2389. doi: 10.1128/iai.63.6.2387-2389.1995

Electrophoretic analysis of the major outer membrane protein of Chlamydia psittaci reveals multimers which are recognized by protective monoclonal antibodies.

M C McCafferty 1, A J Herring 1, A A Andersen 1, G E Jones 1
PMCID: PMC173318  PMID: 7768628

Abstract

Purified major outer membrane protein, detergent solubilized and reduced with dithiothreitol but not heated, gave an apparent molecular weight in sodium dodecyl sulfate (SDS)-polyacrylamide gels almost three times that observed for the heat-denatured SDS-treated peptide. This is similar to the behavior of porin trimers from gram-negative bacteria. Two protective monoclonal antibodies showed strong binding to the proposed trimer but not to denatured, monomeric major outer membrane protein.

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Selected References

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