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pubmed-article:9179290pubmed:abstractTextThe cDNA encoding the 65-kDa subunit of malic enzyme from Ascaris suum was cloned into the bacterial expression vector pKK223-3 and overproduced in Escherichia coli. A protein with a subunit molecular mass of 65,000 was expressed at a level of up to 3% of the total soluble protein in JM109, as judged by SDS-PAGE. The enzyme was purified using column chromatography on phenyl-Sepharose followed by orange-A agarose. The purification procedure resulted in a 32-fold purification with an overall yield of 51%. The bacterially expressed enzyme exhibits kinetic constants identical to those measured for native A. suum NAD-malic enzyme.lld:pubmed
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pubmed-article:9179290pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:9179290pubmed:articleTitleExpression, purification, and characterization of the recombinant NAD-malic enzyme from Ascaris suum.lld:pubmed
pubmed-article:9179290pubmed:affiliationDepartment of Biochemistry and Molecular Biology, University of North Texas Health Science Center at Fort Worth 76107-2699, USA.lld:pubmed
pubmed-article:9179290pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:9179290pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed