[The cell wall of Bacillus brevis producing gramicidin S, a cyclodecapeptide antibiotic].

Gramicidin S is tritiated in Bacillus brevis G.-B. intact cells by activated tritium atoms (which is indicative of its surface localisation). The cell wall protein is tritiated very weakly, which shows that it is screened, apparently, by gramicidin adsorbed on its surface. The cell wall protein is not a glycoprotein and its interaction with exogenous gramicidin S causes cell aggregation. As follows from the Rf value after the chromatographic separation of B. brevis lipids, the reaction of staining, and the data of H-NMR spectroscopy for the fraction of phospholipids, the main membrane phospholipid is an anionic acetylated phosphatidyl ethanolamine.