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Published on: August 3, 2017
Purification of prephenate dehydratase from Corynebacterium glutamicum by affinity chromatography
1School of Chemical Engineering and Materials Science, University of Oklahoma, Norman 73019.
Abstract:
Prephenate dehydratase has been purified from the wild type strain Corynebacterium glutamicum by affinity chromatography. Three ligands, L-Trp, L-Tyr, and L-Phe have been tested as well as conditions for elution. L-Phe is the most specific ligand: it leads to a purification factor of 11 in one step using step gradients of NaCl in Tris-HCl buffer at pH 7.5.

