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J. Biochem, 1976, Vol. 79, No. 6 1381-1383
© 1976 Japanese Biochemical Society

other

Purification, Crystallization, and Some Properties of Creatine Amidinohydrolase from Pseudomonus putida

Tadashi YOSHIMOTO*, Imao OKA** and Daisuke TSURU*

*Faculty of Pharmaceutical Sciences, Nagasaki University Bunkyo-Machi, Nagasaki, Nagasaki 852
**Eiken Kagaku Co. Katsushika-ku, Tokyo 124

A method was developed for purification and crystallization of creatinase [creatine amidinohydrolase, EC 3. 5. 3. 3] from Pseudotnonas putida var. naraensis C-83. The purified preparation appeared homogeneous on disc electrophoresis and ultracentri-fugation and had a molecular weight of 94, 000. It was most active at pH 8 and stable between pH 6 and 8 for 24 hr at 37°. SDS-polyacrylamide gel electrophoresis indicated that the native enzyme was made up of two subunit monomers, the molecular weights of which were estimated to be 47, 000. Inhibition experiments suggested that a sulfhydryl group is located in or near the active site of the enzyme.


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