Abstract
The recombinant murine immune interferon (rMu-IFN-γ) was purified to homogeneity from Escherichia coli harboring the expression vector of murine IFN-γ. The purified rMu-IFN-γ showed an M r of 15000 in SDS-polyacrylamide gel electrophoresis. Results of amino acid analysis, amino- and carboxyl-terminal analyses and peptide mapping of rMu-IFN-γ suggest that it has the complete protein sequence predicted on the basis of cDNA except for lack of four amino acid residues from the mature carboxyl-terminus.
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