1975Agricultural and Biological ChemistryOpen access

Studies on lytic enzyme against cariogenic streptococci. III. Purification and properties of lytic enzymes from Streptomyces globisporus 1829.

Kanae Yokogawa, Shigeo Kawata, T Takemura

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Abstract

Two lytic enzymes capable of lysing Streptococcus mutans have been purified to give a single band on disc-gel electrophoresis, respectively.The M-1 and M-2 enzymes were both proved to be N-acetylmuramidases.However, these enzymes were entirely different on their enzymatic properties.The molecular weights were about 20,000 and 11,000 for M-1 and M-2 enzymes, respectively, The maximal lytic activity of M-1 enzyme was obtained at ionic strength 0.05, while lytic activity of M-2 enzyme did not change within the ionic strength range of 0 to 0.05.The M-1 enzyme constituted the majority of the total lytic activity against the cell walls of Streptococcus mutans BHT of cultured filtrate.The M-2 enzyme showed less specific lytic activity on the cell walls of Streptococcus mutans BHT than M-1 enzyme.

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Two lytic enzymes capable of lysing Streptococcus mutans have been purified to give a single band on disc-gel electrophoresis, respectively.The M-1 and M-2 enzymes were both proved to be N-acetylmuramidases.However, these enzymes were entirely different on their enzymatic properties.The molecular weights were about 20,000 and 11,000 for M-1 and M-2 enzymes, respectively, The maximal lytic activity of M-1 enzyme was obtained at ionic strength 0.05, while lytic activity of M-2 enzyme did not change within the ionic strength range of 0 to 0.05.The M-1 enzyme constituted the majority of the total lytic activity against the cell walls of Streptococcus mutans BHT of cultured filtrate.The M-2 enzyme showed less specific lytic activity on the cell walls of Streptococcus mutans BHT than M-1 enzyme.

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Available abstract

Two lytic enzymes capable of lysing Streptococcus mutans have been purified to give a single band on disc-gel electrophoresis, respectively.The M-1 and M-2 enzymes were both proved to be N-acetylmuramidases.However, these enzymes were entirely different on their enzymatic properties.The molecular weights were about 20,000 and 11,000 for M-1 and M-2 enzymes, respectively, The maximal lytic activity of M-1 enzyme was obtained at ionic strength 0.05, while lytic activity of M-2 enzyme did not change within the ionic strength range of 0 to 0.05.The M-1 enzyme constituted the majority of the total lytic activity against the cell walls of Streptococcus mutans BHT of cultured filtrate.The M-2 enzyme showed less specific lytic activity on the cell walls of Streptococcus mutans BHT than M-1 enzyme.

Key concepts: Lytic cycle, Enzyme, Streptococcus mutans, Lysis, Chemistry, Biochemistry, Microbiology, Streptomyces

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Studies on lytic enzyme against cariogenic streptococci. III. Purification and properties of lytic enzymes from Streptomyces globisporus 1829. — Research Paper | ScholarLens