Egg yolk-derived immunoglobulin (IgY) against Porphyromonas gingivalis 40-kDa outer membrane protein inhibits coaggregation activity.

The anaerobic bacterium Porphyromonas gingivalis, a major pathogen in periodontitis, aggregates with a number of oral bacteria to form dental plaque, which is important for its colonization. We previously cloned the gene coding the 40-kDa outer membrane protein (OMP) of P. gingivalis 381 and produced large amounts of the recombinant (r) protein.

Inhibition of Porphyromonas gingivalis hemagglutinating activity by IgY against a truncated HagA.

Porphyromonas gingivalis has been implicated as an important pathogen in the development of periodontitis. Hemagglutinins have been identified as important adhesion molecules, allowing Porphyromonas gingivalis to adhere to gingival tissue cells, and to attach and lyse erythrocytes in order to uptake Fe ions as essential nutrition. One hemagglutinin, hemagglutinin A (HagA), has been molecularly cloned via functional screening for hemagglutinating activity.

Further development of an electroosmotic medium pump system for preparative disk gel electrophoresis.

A simple and practical 6.8-cm-diameter (36.30-cm(2) cross-sectional-area) preparative disk gel electrophoresis device, based on the design of M.