Purification and characterization of recombinant murine immune interferon.
The recombinant murine immune interferon (rMu-IFN-gamma) was purified to homogeneity from Escherichia coli harboring the expression vector of murine IFN-gamma. The purified rMu-IFN-gamma showed an Mr of 15 000 in SDS-polyacrylamide gel electrophoresis. Results of amino acid analysis, amino- and carboxyl-terminal analyses and peptide mapping of rMu-IFN-gamma 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.
D000595:Amino Acid Sequence; D000818:Animals; D004926:Escherichia coli / Q000032:analysis; D005822:Genetic Vectors; D007371:Interferon-gamma / Q000302:isolation & purification* / Q000378:metabolism; D051379:Mice; D010446:Peptide Fragments / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000378:metabolism
D010446:Peptide Fragments; D011994:Recombinant Proteins; D007371:Interferon-gamma