Expression of mature human interleukin 2 and its derivatives in Escherichia coli and comparison of their biological activity in vitro.
Open Access
- 1 January 1987
- journal article
- Published by Oxford University Press (OUP) in Agricultural and Biological Chemistry
- Vol. 51 (4) , 1135-1142
- https://doi.org/10.1271/bbb1961.51.1135
Abstract
A mature human interleukin 2 (hIL-2) and its derivatives that lacked the N-terminal portion were expressed in Escherichia coli under the control of the phage λ PL promoter. They accumulated in the form of insoluble inclusion bodies and accounted for about 30% of the total cellular protein. The mature hIL-2 and its derivatives were further purified and their in vitro biological activity was compared in an IL-2 microassay. The results suggested that the hIL-2 derivatives without the N-terminal three or five amino acids were as active as intact hIL-2 and that those without the N-terminal eight or nine amino acids were less active than the intact form.Keywords
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