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Article

Isolation and refolding of a mutant methionine-free interleukin-2-receptor alpha chain synthesized as a fusion protein in Escherichia coli.

European journal of biochemistry - 1 Jul 1994

Seipelt I, Engels J W

Abstract excerpt

A soluble domain of the interleukin(IL)-2 receptor, the alpha chain synthesized in Escherichia coli, was employed to study expression and refolding of the protein. The results showed that it is possible to obtain biologically active synthetic methionine-free IL-2 receptor alpha chain (synIL-2R alpha) after BrCN cleavage and renaturation of the crude cleavage material, although the alpha chain is expressed as a...

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PMID: 8033903
DOI: 10.1111/j.1432-1033.1994.tb18993.x

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