Improved protein purification system based on C-terminal cleavage of Npu DnaE split intein.
Alcohol Dehydrogenase
/ chemistry
Biotechnology
/ methods
Chromatography, Affinity
/ instrumentation
DNA Polymerase III
/ genetics
Dithiothreitol
/ chemistry
Escherichia coli
/ metabolism
Green Fluorescent Proteins
/ chemistry
Inteins
Ligands
Protein Domains
Protein Splicing
Recombinant Proteins
/ chemistry
Zinc
/ chemistry
Affinity chromatography
C-terminal cleavage
Npu DnaE intein
Protein purification
Trans-splicing
Journal
Bioprocess and biosystems engineering
ISSN: 1615-7605
Titre abrégé: Bioprocess Biosyst Eng
Pays: Germany
ID NLM: 101088505
Informations de publication
Date de publication:
Nov 2020
Nov 2020
Historique:
received:
25
02
2020
accepted:
17
05
2020
pubmed:
25
5
2020
medline:
3
8
2021
entrez:
25
5
2020
Statut:
ppublish
Résumé
A purification system was constructed with the N-segment of the Npu DnaE split intein as an affinity ligand immobilized onto an epoxy-activated medium and the C-segment used as the cleavable tag fusing target protein. The affinity properties of C-tagged proteins adsorbed on I
Identifiants
pubmed: 32447513
doi: 10.1007/s00449-020-02382-w
pii: 10.1007/s00449-020-02382-w
doi:
Substances chimiques
Ligands
0
Recombinant Proteins
0
Green Fluorescent Proteins
147336-22-9
Alcohol Dehydrogenase
EC 1.1.1.1
DNA polymerase III, alpha subunit
EC 2.7.7.-
DNA Polymerase III
EC 2.7.7.7
Zinc
J41CSQ7QDS
Dithiothreitol
T8ID5YZU6Y
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
1931-1941Subventions
Organisme : National Key R&D Program of China
ID : Grant No. 2018YFC1603202/2018YFC1603200