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

Journal article

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...

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Authors: Delves, C; Ballantine, S; Tansik, R; Baccanari, D; Stammers, D

• Publication status: Published
• Journal: Protein expression and purification
• Volume: 4
• Issue: 1
• Pages: 16-23
• Publication date: 1993-02-01
• DOI: 10.1006/prep.1993.1003
• EISSN: 1096-0279
• ISSN: 1046-5928
• Language: English
• Keywords: Amino Acid Sequence; NADP; Base Sequence; Cloning, Molecular; Pneumocystis; Protein Folding; DNA; Solubility; Polymerase Chain Reaction; Escherichia coli; Molecular Sequence Data; Recombinant Proteins; Tetrahydrofolate Dehydrogenase; Folic Acid Antagonists