Tag Archives: lipopolysaccharides
Influence of lipopolysaccharides of Escherichia coli on the protease activity of several Bacillus strains
L. D. Varbanets1, O. S. Brovarska1, O. V. Gudzenko1*,
K. G. Garkava2, A. R. Makarenko2
1Institute of Microbiology and Virology named after D. K. Zabolotny,
National Academy of Sciences of Ukraine, Kyiv, Ukraine;
2National Technical University of Ukraine
“Igor Sykorsky Kyiv Polytechnic Institute”, Kyiv, Ukraine;
*e-mail: alena.gudzenko81@gmail.com
Received: 07 July 2025; Revised: 23 August 2025;
Accepted: 12 September 2025; Available on-line: 17 September 2025
We have previously shown that lipopolysaccharides (LPS) of a number of strains of the phytopathogenic species Pantoea agglomerans are capable of increasing the activity of Bacillus peptidases with fibrinolytic, elastase and collagenase activities by 2-4 times. The aim of this work was to investigate the effect of isolated intracellular LPS1 and extracellular LPS2 of Escherichia coli on the activity of purified bacilli proteases with elastase and fibrinogenolytic activity. It was shown that both LPS2 and LPS1 of E. coli 23 can increase the elastase activity of Bacillus sp. IMV B-7883 by 600 and 416% respectively. Both LPS are able to increase fibrinogenolytic activity in all studied Bacillus strains, but its greatest stimulation (200%) was observed under the action of LPS2 of Bacillus sp. L9.
Avidity and competitive inhibition of binding native and chaotropically modified immunoglobulins with protein and glycolipid antigens
N. V. Khimich, A. I. Gоrdienko
State Institution S. I. Georgievsky Crimea State Medical University, Simferopol, Ukraine;
e-mail: uu4jey@csmu.strace.net
It is established, that native and chaotropically modified immunoglobulins essentially differ by avidity and character of competitive inhibition of binding with protein (оvalbumin), glycolipid (lipopolysaccharides) antigens and native double-string DNA. Apparently, it is connected with structural and functional distinctions of their antigen-binding centres.