Jun 1, 1976

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

Journal of Biochemistry
T YoshimotoD Tsuru

Abstract

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.

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Mentioned in this Paper

Macromolecular Compounds
Polyacrylamide Gels
Pseudomonas putida
Sulfhydryl Compounds
Creatine
Site
Electrophoresis, Disc
Hydrolase
Purification Aspects
Metabolic Inhibition

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