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pubmed-article:11388802pubmed:abstractTextA 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.lld:pubmed
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pubmed-article:11388802pubmed:articleTitleExpression and purification of Escherichia coli beta-glucuronidase.lld:pubmed
pubmed-article:11388802pubmed:affiliationDepartment of Biochemistry, College of Medicine, University of Saskatchewan, 107 Wiggins Road, Saskatoon, Saskatchewan S7N 5E5, Canada.lld:pubmed
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pubmed-article:11388802pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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