title: Purification of prephenate dehydratase from Corynebacterium glutamicum by affinity chromatography.
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.
authors.affiliation: School of Chemical Engineering and Materials Science, University of Oklahoma, Norman 73019.
authors.forename: S
authors.initials: S
authors.lastname: Bertaux
authors.forename: R G
authors.initials: RG
authors.lastname: Harrison
mesh_terms: D002846:Chromatography, Affinity; D003352:Corynebacterium / Q000201:enzymology*; D010649:Phenylalanine; D011303:Prephenate Dehydrogenase / Q000302:isolation & purification*; D014364:Tryptophan; D014443:Tyrosine
chemical_list: D014443:Tyrosine; D010649:Phenylalanine; D014364:Tryptophan; D011303:Prephenate Dehydrogenase