Factors affecting the synthesis of the n-terminal methionine-free molecule of recombinant human interleukin-2 by Escherichia coli
- 1 January 1988
- journal article
- research article
- Published by Elsevier in Journal of Fermentation Technology
- Vol. 66 (2) , 181-185
- https://doi.org/10.1016/0385-6380(88)90045-3
Abstract
No abstract availableThis publication has 16 references indexed in Scilit:
- Separation of recombinant human interleukin-2 and methionyl interleukin-2 produced in EscherichiacoliBiochemical and Biophysical Research Communications, 1986
- High-Level Expression inEscherichia coliof Biologically Active Bovine Growth HormoneDNA, 1985
- Characterization of human interleukin 2 derived from Escherichia coliBiochemical Journal, 1985
- Purification and characterization of recombinant human interleukin-2 produced in Escherichia coliBiochemical and Biophysical Research Communications, 1985
- Interleukin 2Annual Review of Immunology, 1984
- Structure and expression of a cloned cDNA for human interleukin-2Nature, 1983
- Molecular cloning of human interleukin 2 cDNA and its expression inE. coliNucleic Acids Research, 1983
- Purified human growth hormone from E. coli is biologically activeNature, 1981
- Properties of a Human Alpha-Interferon Purified fromE. ColiExtractsJournal of Interferon Research, 1981
- Nitrogen Fixation in Grasses Inoculated with Spirillum lipoferumScience, 1976