Heat Activation of Muramidase
1963 年 53 巻 5 号 p. 374-380
詳細
1963 年 53 巻 5 号 p. 374-380
1. An increase in the hydrolytic activity of muramidase against glycol chitin, the sub-strate, was observed when the muramidase
solution was heated in a high temperature bath for several hours.
2. The increases in the activity of mura-midase on heating depend on the condition used such as the temperature of bath, the heating time, pH and ionic strength of buffer solution and solute concentration.
3. The heat activation of muramidase depends also on the history of muramidase preparation.
4. The heat activation is reversible with respect to tqe temperature. Activated mura-midase reduced its activity to the original one when the activated muramidase was stored in a cold room for 48 hours.
5. No change in the ordinary molecular properties of the treated muramidase was observed. This fact will suggest that the heat activation is caused by the undetected struc-tural rearrangement of the active site of the muramidase molecule.
The authors are indebted to Dr. S. Akabori for encouragement and are very grateful to Dr. T. Isemura for kind support during the period in which these ex-periments were done in the Institute for Protein Research, Osaka University, and to Dr. C. C. Bigelow for the valuable advices. The authors also would like to thank to Mr. T. Yamamoto and Mrs. K. Imai for their help in this work.
