Work

Expression in Escherichia coli of chemically synthesized genes for human insulin.

Year: 1979

Type: article

Abstract: Synthetic genes for human insulin A and B chains were cloned separately in plasmid pBR322. The cloned synthetic genes were then fused to an Escherichia coli beta-galactosidase gene to provide efficient transcription and translation and a stable precursor protein. The insulin peptides were cleaved from beta-galactosidase, detected by radioimmunoassay, and purified. Complete purification of the A chain and partial purification of the B chain were achieved. These products were mixed, reduced, and reoxidized. The presence of insulin was detected by radioimmunoassay.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.76.1.106

Authors: D V Goeddel, D G Kleid, F Bolivar, H L Heyneker, D G Yansura, R Crea, T Hirose, A Kraszewski, K Itakura, A D Riggs

Institutions: City Of Hope National Medical Center, Genentech

Language: English

Topic: Protein purification and stability

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

OpenAlex ID: W2015139192

FWCI: 12.13

Cites: 15

Cited by: 870

Related to: 10