Abstract
The effect of various compounds on the activity and stability of a phage-associated enzyme lysing cells of streptococci of groups A and C (PlyC) was investigated. Substantial inhibition of the enzyme activity was revealed at an increased ionic strength (in the presence of NaCl) and upon the addition of carbohydrates (mono-, di-, and polysaccharides), i.e., agents stabilizing many enzymes. It was established that the enzyme activity was substantially reduced in the presence of positively charged polyelectrolytes and surfactants, whereas incubation with micelle-forming substances and negatively charged polyelectrolytes led to PlyC activation and stabilization. It was shown that, in the micellar polyelectrolyte composition M16, the enzyme retained its activity for 2 months; while in a buffer solution under the same conditions (pH 6.3, room temperature), ture), it practically completely lost its activity in 2 days. Characteristics of the enzyme thermal inactivation were found, in particular, its half-inactivation time at various temperatures; these allowed us to estimate its behavior at any temperature and to recommend conditions for its storage and use.
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Abbreviations
- CPC:
-
cetylpyridinium chloride
- PAA:
-
polyacrylic acid
- PlyC:
-
phage-associated enzyme lysing streptococcal cells of A and C groups
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Original Russian Text © N.L. Klyachko, N.F. Dmitrieva, A.S. Eshchina, O.V. Ignatenko, L.Yu. Filatova, E.I. Rainina, A.K. Kazarov, A.V. Levashov, 2008, published in Bioorganicheskaya Khimiya, 2008, Vol. 34, No. 3, pp. 416–421.
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Klyachko, N.L., Dmitrieva, N.F., Eshchina, A.S. et al. Bacteriophage enzymes for the prevention and treatment of bacterial infections: Stability and stabilization of the enzyme lysing Streptococcus pyogenes cells. Russ J Bioorg Chem 34, 375–379 (2008). https://doi.org/10.1134/S1068162008030217
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DOI: https://doi.org/10.1134/S1068162008030217