Abstract
The physico-chemical and enzymatic properties of muramidase in aqueous so-lutions of ethylene glycol, polyethylene glycol and sucrose have been examined. Ethylene glycol and polyethylene glycol disrupt neither the helical structure nor the hydrophobic region of the muramidase molecule.
The activity of muramidase does not change in the presence of sucrose or glycerine. However, ethylene glycol, dioxane, dimethyl-sulfoxide, and N, N-dimethylformamide de-crease the activity in the concentration range where no structural change of the molecule can be detected.
The authors are indebted to Prof. T. Isemura for his encouragement. They also wish to thank Dr. T. Takagi for discussions.
