Purification, Crystallization, and Some Properties of Creatine Amidinohydrolase from Pseudomonus putida
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説明
A method was developed for purification and crystallization of creatinase [creatine amidinohydrolase, EC 3.5.3.3] 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.
収録刊行物
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- The Journal of Biochemistry
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The Journal of Biochemistry 79 1381-1383, 1976-06-01
Oxford University Press (OUP)