Expression and purification of Escherichia coli beta-glucuronidase |
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Authors: | Aich S Delbaere L T Chen R |
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Institution: | Department of Biochemistry, College of Medicine, University of Saskatchewan, 107 Wiggins Road, Saskatoon, Saskatchewan S7N 5E5, Canada. |
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Abstract: | A strong and constitutive expression vector of Escherichia coli beta-glucuronidase with the isocitrate dehydrogenase promoter has been developed for producing a large amount of recombinant protein. More than 95% pure enzyme was obtained by a four step purification procedure-ammonium sulfate precipitation, DEAE ion-exchange chromatography, Superose 12 gel filtration, and hydroxyapatite steric ion-exchange chromatography. The overexpressed gene can produce 23 mg of pure enzyme from one liter of bacterial culture. |
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