[Isolation and evaluation of properties of muramidase causing the lysis of group A streptococci].
Muramidase which actively lyses the cell walls of group A hemolytic streptococci has been isolated from the culture fluid of Actinomyces levoris by precipitation on ammonium sulfate, gel filtration on Sephadex G-25, ion exchange chromatography on DEAE cellulose and double electrofocusing. The enzyme thus obtained has shown its maximum activity at 40-50 degrees C. At 60 degrees C muramidase was completely inactivated. The enzyme has a wide range of optimum pH values: 5.0-9.5. The highest percentage of lysis of streptococcal cell walls has been observed in plycine-NaOH and potassium phosphate buffers at pH 8.0. Muramidase completely lysed Streptococcus pyogenes cells of different serological groups except enterococci (group D) and staphylococci. This sign allows to differentiate group D streptococcus from streptococci of other groups.
D000190:Actinomyces / Q000201:enzymology; D002473:Cell Wall / Q000187:drug effects; D007525:Isoelectric Focusing; D009113:Muramidase / Q000302:isolation & purification* / Q000494:pharmacology; D012703:Serotyping; D013211:Staphylococcus aureus / Q000187:drug effects; D013291:Streptococcus / Q000145:classification / Q000187:drug effects*
D009113:Muramidase
Poluchenie i izuchenie muramidazy, liziruiushcheĭ streptokokk gruppy A.