Journal article icon

Journal article

Refolding of recombinant Pneumocystis carinii dihydrofolate reductase and characterization of the enzyme.

Abstract:

The isolation of dihydrofolate reductase (DHFR) cDNA sequences from the messenger RNA of Pneumocystis carinii using the polymerase chain reaction is described. The 206-amino acid P. carinii DHFR was expressed to high levels in Escherichia coli inclusion bodies using the T7 promoter expression system. Solubilization of the inclusion bodies in 4 M guanidine hydrochloride and refolding of the recombinant protein in the presence of 0.5% polyethylene glycol 1450 yielded correctly folded DHFR which...

Expand abstract
Publication status:
Published

Actions


Access Document


Publisher copy:
10.1006/prep.1993.1003

Authors


More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Biology
Role:
Author
Journal:
Protein expression and purification
Volume:
4
Issue:
1
Pages:
16-23
Publication date:
1993-02-05
DOI:
EISSN:
1096-0279
ISSN:
1046-5928
URN:
uuid:e63077ee-b0bf-40c5-8200-1919d64a7d22
Source identifiers:
72678
Local pid:
pubs:72678

Terms of use


Metrics


Views and Downloads






If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP