β--Acetylglucosaminidase has been purified from the walls of 168 and compared with the other known autolysin, -acetylmuramyl--alanine amidase (amidase). The β--acetylglucosaminidase was a dimer in LiCl buffers with a sub-unit molecular weight of 90000 and a pH optimum of about 5.0. It was very sensitive to proteolytic enzymes and was critically activated by 0.1 to 0.2 -LiCl. It was insoluble in concentrations of LiCl lower than 0.05 to 0.1 . It was less strongly bound to walls than was the amidase, which was a monomer of molecular weight 30000 to 40000 in LiCl buffers. The β--acetylglucosaminidase is an endoenzyme and showed no exo-activity. Lysozyme-like enzyme (muramidase) activity was undetectable in the wall extracts examined.


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