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Availability of dihydrofolate reductase affinity handle in expressing human prolactin as a soluble fusion protein.

Research paper by M M Iwakura, M M Morikawa

Indexed on: 01 Nov '93Published on: 01 Nov '93Published in: Bioscience, biotechnology, and biochemistry



Abstract

Human prolactin (PRL) cDNA was successfully expressed in Escherichia coli cells with the aid of a dihydrofolate reductase (DHFR) affinity handle. The formed DHFR-PRL fusion protein was accumulated in E. coli cells as a soluble protein with DHFR activity at 30 degrees C. The fusion protein was highly purified with monitored the DHFR activity by methotrexate-bound affinity chromatography, suggesting the usefulness of the handle even in expressing a large polypeptide as a fusion protein.