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

[摘要] 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 beta-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. (C) 1998 Elsevier Science Ltd. All rights reserved.

[发布日期] 1998-12-24

[关键词] beta-lactam antibiotics;biosynthesis;protein purification;affinity chromotography