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J Biochem. 1976 Jun;79(6):1381-3.

Purification, crystallization, and some properties of creatine amidinohydrolase from Pseudomonas putida.


A method was developed for purification and crystallization of creatinase [creatine amidinohydrolase, EC] from Pseudomonas putida var. naraensis C-83. The purified preparation appeared homogeneous on disc electrophoresis and ultracentrifugation 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 degrees. 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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