Abstract
Hen's egg white muramidase was reduced by sodium thioglycolate in 8M urea to give an unfolded linear polypeptide having eight sulfhydryl groups. The deformation of the molecular structure could be reversed by removal of thioglycolate, dilution of urea, and air-oxidation under appropriate conditions to give completely renatured muramid-ase in a good yield. The completely renatured muramidase was isolated by crystallization, and its various properties coincid-ed well with those of native muramidase.
This finding suggests that the informations for the secondary and tertiary structures of muramidase are contained in the primary structure.
The authors wish to express their thanks to Prof. M. Funatsu and Dr. K. Hayashi of Kyushu University who supplied us glycol chitin, and to Dr. K. Harnaguchi for his kind suggestions. Our thanks are also due to Miss. H. Nishibayashi for the analysis of cysteine.
