Inhibitors of an AdoMet-dependent 3-amino-3-carboxypropyl transferase and their use as ligands for protein affinity chromatography

Article abstract of DOI:10.1016/S0040-4020(98)01004-7

The screening of potential affinity ligands and the development of a two-stage affinity purification of an S-adenosylmethionine-dependent 3- amino-3-carboxypropyl transferase involved in the biosynthesis of the β- lactam antibiotic nocardicin A is described from a cell-free extract of Nocardia uniformis subsp. tsuyamanesis. This protein is particularly sensitive to ion exchange and salt effects necessitating a pair of neutral ligands to be used in the final purification.