title: Electrophoretic analysis of the major outer membrane protein of Chlamydia psittaci reveals multimers which are recognized by protective monoclonal antibodies.
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.
authors.affiliation: Moredun Research Institute, Edinburgh, United Kingdom.
authors.forename: M C
authors.initials: MC
authors.lastname: McCafferty
authors.forename: A J
authors.initials: AJ
authors.lastname: Herring
authors.forename: A A
authors.initials: AA
authors.lastname: Andersen
authors.forename: G E
authors.initials: GE
authors.lastname: Jones
mesh_terms: D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology*; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000276:immunology / Q000302:isolation & purification; D002691:Chlamydophila psittaci / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D051379:Mice
chemical_list: D000911:Antibodies, Monoclonal; D001425:Bacterial Outer Membrane Proteins