title: Availability of dihydrofolate reductase affinity handle in expressing human prolactin as a soluble fusion protein.
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.
authors.affiliation: National Institute of Bioscience and Human-Technology, Ibaraki, Japan.
authors.forename: M
authors.initials: M
authors.lastname: Iwakura
authors.forename: M
authors.initials: M
authors.lastname: Morikawa
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D002846:Chromatography, Affinity; D018076:DNA, Complementary / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D004926:Escherichia coli / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D011388:Prolactin / Q000096:biosynthesis* / Q000235:genetics; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis*; D013762:Tetrahydrofolate Dehydrogenase / Q000235:genetics*
chemical_list: D018076:DNA, Complementary; D011993:Recombinant Fusion Proteins; D011388:Prolactin; D013762:Tetrahydrofolate Dehydrogenase