Agricultural and Biological Chemistry
Online ISSN : 1881-1280
Print ISSN : 0002-1369
ISSN-L : 0002-1369
Purification and Properties of Lytic Enzymes from Streptomyces globisporus 1829
Kanae YOKOGAWAShigeo KAWATATadashi TAKEMURA
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1975 Volume 39 Issue 8 Pages 1533-1543

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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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