Studies on lytic enzyme against cariogenic streptococci. III. Purification and properties of lytic enzymes from Streptomyces globisporus 1829.
Kanae Yokogawa, Shigeo Kawata, T Takemura
Abstract
Open-access reader
Kanae Yokogawa, Shigeo Kawata, T Takemura
Abstract
Open-access reader
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.
OpenAlex reports 114 citations for this work. Citation counts describe recorded attention and do not establish research quality.
A contribution statement is not available in the OpenAlex record.
Method details are not available in the OpenAlex metadata.
Findings are not separately available in the OpenAlex metadata.
Limitations are not available in the OpenAlex metadata.
Application details are not available in the OpenAlex metadata.
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