[Detection of AlpA and AlpB lytic endopeptidase propeptides of Lysobacter sp. XL1 by sandwich-enzyme immunoassay based on monoclonal antibodies].

The extracellular lytic endopeptidases AlpA and AlpB of the bacterium Lysobacter sp. XL1 are highly homologous and synthesized as precursors consisting of signal peptide, propeptide and mature form. In this work, two monoclonal antibodies against propeptide endopeptidase AlpA (ProA) and eleven against propeptide endopeptidase AlpB (ProB) were obtained to study the AlpA and AlpB endopeptidases secretion.

[Effect of the proteolytic enzymes of Bacillus licheniformis and the lysoamidase of Lysobacter sp. XL1 on Proteus vulgaris and Proteus mirabilis].

Preparations of culture liquid of three Bacullus licheniformis strains (S, 103, and 60.4) and the enzymatic preparation lysoamidase from culture liquid of Lysobacter sp. strain XL1 actively lysed preliminarily autoclaved cells of gram-negative bacteria Proteus vulgaris and P.

[Mechanism of action of the extracellular bacteriolytic enzymes of Lysobacter sp. on gram-positive bacteria: role of the cell wall anionic polymers of the target bacteria].

The study of the extracellular bacteriolytic enzymes of Lysobacter sp. showed that they can efficiently hydrolyze the peptidoglycan of gram-positive bacteria provided that there is an electrostatic interaction of these enzymes with the cell wall anionic polymers, teichoic and teichuronic acids in particular. The hydrolytic action of bacteriolytic enzymes on the cell wall largely depends on the negative charge of teichoic and teichuronic acids, rather than on their chemical composition.

[The effect of the extracellular bacteriolytic enzymes of Lysobacter sp. on gram-negative bacteria].

The effect of the extracellular bacteriolytic enzymes of Lysobacter sp. on gram-negative bacteria was studied. These enzymes were found to be able to hydrolyze the peptidoglycan that was isolated from the gram-negative bacteria, the hydrolysis being completely inhibited by the cell wall lipopolysaccharide of these bacteria.