Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10843914 | Protein Expression and Purification | 2005 | 4 Pages |
Abstract
The bi-functional enzyme, adenosylcobinamide kinase/adenosylcobinamide-phosphate guanylyltransferase (CobU), is involved in the biosynthesis of cobalamin in Salmonella typhimurium, and, therefore, can be used for the in vitro synthesis of analogs of B12. Previously, five different steps were required to purify the recombinant enzyme from Escherichia coli. Here, we describe the cloning, sequencing, and expression of the cobU gene from S. typhimurium ATCC 19585 and, without introducing a purification tag sequence to the N- or C-terminus of the recombinant enzyme, a new single-step purification method based on hydrophobic interaction chromatography.
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Authors
Fang-Ciao Hsu, Tsung-Jung Ho, Chien-Chen Lai, Chin-Fen Lin, Hao-Ping Chen,