title: Single-process expression and purification of multiple recombinant proteins through cocultivation and affinity purification.
abstract: Multiple recombinant proteins can be expressed simultaneously by inoculating multiple seed cultures into a single growth medium and inducing protein expression at a single time point. Up to three recombinant proteins can be individually purified from such a mixed culture (cocultivation) through the use of a combination of a multihistidine and a modified intein as affinity tags and the Ni sepharose and chitin as affinity matrices. This method may facilitate the study of protein complexes by rapidly obtaining multiple protein components in a single process and may potentially increase the efficiency of recombinant protein production at research and industrial scales.
authors.affiliation: New England Biolabs, 240 County Road, Ipswich, MA 01938, USA.
authors.forename: Mathieu
authors.initials: M
authors.lastname: Porte
authors.forename: Shaorong
authors.initials: S
authors.lastname: Chong
mesh_terms: D001671:Biochemistry / Q000379:methods*; D002846:Chromatography, Affinity; D018920:Coculture Techniques; D006639:Histidine; D047668:Inteins; D009842:Oligopeptides; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis* / Q000235:genetics / Q000302:isolation & purification*
chemical_list: C471213:His-His-His-His-His-His; D009842:Oligopeptides; D011993:Recombinant Fusion Proteins; D006639:Histidine