Abstract
We attempted to purify the K-agglutinogen of Bordetella pertussis by mild procedures. From the supernatant of sonic treated cells, the K-agglutinogen was separated by a successive use of O-diethylaminoethyl (DEAE)-cellulose column chromatography, ammonium sulfate precipitation and O-carboxymethyl (CM)-cellulose column chromatography. The specific activity of purified K-agglutinogen increased 64-128 fold without damaging either the L or S antigens, and recovery was about 86%. A fraction containing mainly S-agglutinogen, was also obtained. The K-agglutinogen, which was a simple protein with an S value of 2.5, was confirmed to be in a highly purified state by a gel-diffusion test, K-antibody production and physicochemical tests, and was also found to be free from other biologically active substances of B. pertussis: namely heat labile toxin, hemagglutinin, histamine-sensitizing factor and O-antigen. No protective activity was found in the purified K-agglutinogen or against intracerebral challenge with B. pertussis in mice.
