[The isolation and partial characterization of the cell wall proteins of Listeria monocytogenes]

The preparative scheme for the purification of proteins with molecular weights of 39 and 79 kD, obtained from L. monocytogenes membrane fractions, has been developed. This technology included the cultivation of bacteria in heart-brain broth, isolation of bacterial membranes, the extraction of their components with Triton-X-100 and chromatography on Superose columns. The purified proteins have been shown to form structures with a molecular weight of 500-100 kD and pl 4.7 in water solutions.