Production of functional chick liver HMG 2a protein in Escherichia coli.
FEBS Lett
; 367(1): 49-52, 1995 Jun 19.
Article
in En
| MEDLINE
| ID: mdl-7601282
ABSTRACT
An efficient Escherichia coli system for the production of a variant form of high-mobility group-2a protein (HMG 2a), having the additional 5 amino acid residues (Ala-Pro-Thr-Leu-Glu) at the NH2-terminal, has been constructed. cDNA encoding HMG 2a was ligated with the Omp A signal peptide sequence and was inserted into an inducible bacterial expression vector pSH-L. After the plasmid introduced into E. coli was expressed by temperature shift, the recombinant product was purified by trichloacetic acid precipitation followed by Bio-Rex 70 column chromatography. The purified product showed the expected NH2-terminal sequence and the superhelical activity of circular DNA similar to the authentic HMG 2a isolated from chick liver.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
High Mobility Group Proteins
/
Escherichia coli
Limits:
Animals
Language:
En
Journal:
FEBS Lett
Year:
1995
Document type:
Article
Affiliation country: